Full text data of PGLS
PGLS
[Confidence: low (only semi-automatic identification from reviews)]
6-phosphogluconolactonase; 6PGL; 3.1.1.31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
6-phosphogluconolactonase; 6PGL; 3.1.1.31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95336
ID 6PGL_HUMAN Reviewed; 258 AA.
AC O95336;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=6-phosphogluconolactonase;
DE Short=6PGL;
DE EC=3.1.1.31;
GN Name=PGLS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10518023; DOI=10.1016/S0014-5793(99)01247-8;
RA Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M.,
RA van Schaftingen E.;
RT "Identification of the cDNA encoding human 6-phosphogluconolactonase,
RT the enzyme catalyzing the second step of the pentose phosphate
RT pathway.";
RL FEBS Lett. 459:223-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 41-72 AND 82-96, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-242.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-
CC phosphogluconate.
CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-
CC phospho-D-gluconate.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72960.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ243972; CAB57866.1; -; mRNA.
DR EMBL; BC014006; AAH14006.1; -; mRNA.
DR EMBL; AF091091; AAC72960.1; ALT_INIT; mRNA.
DR RefSeq; NP_036220.1; NM_012088.2.
DR UniGene; Hs.466165; -.
DR ProteinModelPortal; O95336; -.
DR SMR; O95336; 38-247.
DR MINT; MINT-5000838; -.
DR STRING; 9606.ENSP00000252603; -.
DR PhosphoSite; O95336; -.
DR OGP; O95336; -.
DR REPRODUCTION-2DPAGE; IPI00029997; -.
DR PaxDb; O95336; -.
DR PeptideAtlas; O95336; -.
DR PRIDE; O95336; -.
DR DNASU; 25796; -.
DR Ensembl; ENST00000252603; ENSP00000252603; ENSG00000130313.
DR GeneID; 25796; -.
DR KEGG; hsa:25796; -.
DR UCSC; uc002ngw.3; human.
DR CTD; 25796; -.
DR GeneCards; GC19P017622; -.
DR HGNC; HGNC:8903; PGLS.
DR HPA; HPA040744; -.
DR HPA; HPA042032; -.
DR MIM; 604951; gene.
DR neXtProt; NX_O95336; -.
DR PharmGKB; PA33240; -.
DR eggNOG; COG0363; -.
DR HOGENOM; HOG000256285; -.
DR HOVERGEN; HBG000030; -.
DR InParanoid; O95336; -.
DR KO; K01057; -.
DR OMA; TYGLYKS; -.
DR OrthoDB; EOG7RZ5QV; -.
DR PhylomeDB; O95336; -.
DR BRENDA; 3.1.1.31; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00115; UER00409.
DR GenomeRNAi; 25796; -.
DR NextBio; 46981; -.
DR PRO; PR:O95336; -.
DR ArrayExpress; O95336; -.
DR Bgee; O95336; -.
DR CleanEx; HS_PGLS; -.
DR Genevestigator; O95336; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 258 6-phosphogluconolactonase.
FT /FTId=PRO_0000090078.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 180 180 N6-acetyllysine.
SQ SEQUENCE 258 AA; 27547 MW; A753FB7E662116DD CRC64;
MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA
AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE
EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK
PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL
DEAAARLLTV PFEKHSTL
//
ID 6PGL_HUMAN Reviewed; 258 AA.
AC O95336;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=6-phosphogluconolactonase;
DE Short=6PGL;
DE EC=3.1.1.31;
GN Name=PGLS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10518023; DOI=10.1016/S0014-5793(99)01247-8;
RA Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M.,
RA van Schaftingen E.;
RT "Identification of the cDNA encoding human 6-phosphogluconolactonase,
RT the enzyme catalyzing the second step of the pentose phosphate
RT pathway.";
RL FEBS Lett. 459:223-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 41-72 AND 82-96, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-242.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-
CC phosphogluconate.
CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6-
CC phospho-D-gluconate.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72960.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ243972; CAB57866.1; -; mRNA.
DR EMBL; BC014006; AAH14006.1; -; mRNA.
DR EMBL; AF091091; AAC72960.1; ALT_INIT; mRNA.
DR RefSeq; NP_036220.1; NM_012088.2.
DR UniGene; Hs.466165; -.
DR ProteinModelPortal; O95336; -.
DR SMR; O95336; 38-247.
DR MINT; MINT-5000838; -.
DR STRING; 9606.ENSP00000252603; -.
DR PhosphoSite; O95336; -.
DR OGP; O95336; -.
DR REPRODUCTION-2DPAGE; IPI00029997; -.
DR PaxDb; O95336; -.
DR PeptideAtlas; O95336; -.
DR PRIDE; O95336; -.
DR DNASU; 25796; -.
DR Ensembl; ENST00000252603; ENSP00000252603; ENSG00000130313.
DR GeneID; 25796; -.
DR KEGG; hsa:25796; -.
DR UCSC; uc002ngw.3; human.
DR CTD; 25796; -.
DR GeneCards; GC19P017622; -.
DR HGNC; HGNC:8903; PGLS.
DR HPA; HPA040744; -.
DR HPA; HPA042032; -.
DR MIM; 604951; gene.
DR neXtProt; NX_O95336; -.
DR PharmGKB; PA33240; -.
DR eggNOG; COG0363; -.
DR HOGENOM; HOG000256285; -.
DR HOVERGEN; HBG000030; -.
DR InParanoid; O95336; -.
DR KO; K01057; -.
DR OMA; TYGLYKS; -.
DR OrthoDB; EOG7RZ5QV; -.
DR PhylomeDB; O95336; -.
DR BRENDA; 3.1.1.31; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00115; UER00409.
DR GenomeRNAi; 25796; -.
DR NextBio; 46981; -.
DR PRO; PR:O95336; -.
DR ArrayExpress; O95336; -.
DR Bgee; O95336; -.
DR CleanEx; HS_PGLS; -.
DR Genevestigator; O95336; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 258 6-phosphogluconolactonase.
FT /FTId=PRO_0000090078.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 180 180 N6-acetyllysine.
SQ SEQUENCE 258 AA; 27547 MW; A753FB7E662116DD CRC64;
MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA
AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE
EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK
PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL
DEAAARLLTV PFEKHSTL
//
MIM
604951
*RECORD*
*FIELD* NO
604951
*FIELD* TI
*604951 6-@PHOSPHOGLUCONOLACTONASE; PGLS
;;6@PGL; 6PGL
*FIELD* TX
CLONING
6-Phosphogluconolactonase (EC 3.1.1.31) catalyzes the hydrolysis of
read more6-phosphogluconolactone, which is the second step of the pentose
phosphate pathway. The bacterial devB gene, which is often found in
proximity to the glucose-6-phosphate dehydrogenase gene (G6PD), encodes
a protein that is homologous to the C-terminal part of human
hexose-6-phosphate dehydrogenase (H6PD; 138090). By searching a human
EST database for cDNAs encoding homologs of the devB protein from A.
actinomycetemcomitans, Collard et al. (1999) identified PGLS cDNAs. They
isolated a human liver cDNA containing a complete PGLS coding sequence.
The deduced 258-amino acid PGLS protein has a calculated molecular mass
of 27,529 Da. PGLS shares 33 to 37% amino acid sequence identity with
yeast Sol1 to Sol4, 26% identity with the C-terminal part of human H6PD,
20 to 25% identity with bacterial devB proteins, and 17% identity with
human glucosamine-6-phosphate isomerase.
MAPPING
By radiation hybrid mapping, Collard et al. (1999) mapped the PGLS gene
to 19p13.2.
*FIELD* RF
1. Collard, F.; Collet, J.-F.; Gerin, I.; Veiga-da-Cunha, M.; Van
Schaftingen, E.: Identification of the cDNA encoding human 6-phosphogluconolactonase,
the enzyme catalyzing the second step of the pentose phosphate pathway. FEBS
Lett. 459: 223-226, 1999.
*FIELD* CD
Patti M. Sherman: 5/11/2000
*FIELD* ED
carol: 07/24/2012
alopez: 8/4/2003
mcapotos: 5/16/2000
psherman: 5/11/2000
*RECORD*
*FIELD* NO
604951
*FIELD* TI
*604951 6-@PHOSPHOGLUCONOLACTONASE; PGLS
;;6@PGL; 6PGL
*FIELD* TX
CLONING
6-Phosphogluconolactonase (EC 3.1.1.31) catalyzes the hydrolysis of
read more6-phosphogluconolactone, which is the second step of the pentose
phosphate pathway. The bacterial devB gene, which is often found in
proximity to the glucose-6-phosphate dehydrogenase gene (G6PD), encodes
a protein that is homologous to the C-terminal part of human
hexose-6-phosphate dehydrogenase (H6PD; 138090). By searching a human
EST database for cDNAs encoding homologs of the devB protein from A.
actinomycetemcomitans, Collard et al. (1999) identified PGLS cDNAs. They
isolated a human liver cDNA containing a complete PGLS coding sequence.
The deduced 258-amino acid PGLS protein has a calculated molecular mass
of 27,529 Da. PGLS shares 33 to 37% amino acid sequence identity with
yeast Sol1 to Sol4, 26% identity with the C-terminal part of human H6PD,
20 to 25% identity with bacterial devB proteins, and 17% identity with
human glucosamine-6-phosphate isomerase.
MAPPING
By radiation hybrid mapping, Collard et al. (1999) mapped the PGLS gene
to 19p13.2.
*FIELD* RF
1. Collard, F.; Collet, J.-F.; Gerin, I.; Veiga-da-Cunha, M.; Van
Schaftingen, E.: Identification of the cDNA encoding human 6-phosphogluconolactonase,
the enzyme catalyzing the second step of the pentose phosphate pathway. FEBS
Lett. 459: 223-226, 1999.
*FIELD* CD
Patti M. Sherman: 5/11/2000
*FIELD* ED
carol: 07/24/2012
alopez: 8/4/2003
mcapotos: 5/16/2000
psherman: 5/11/2000