ID A0A3B3XSX9_9TELE Unreviewed; 513 AA.
AC A0A3B3XSX9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000018189.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000018189.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. {ECO:0000256|RuleBase:RU362120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000256|ARBA:ARBA00001220};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC Evidence={ECO:0000256|ARBA:ARBA00001220};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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DR RefSeq; XP_014837215.1; XM_014981729.1.
DR STRING; 48701.ENSPMEP00000032908; -.
DR Ensembl; ENSPMET00000027271.1; ENSPMEP00000032908.1; ENSPMEG00000021159.1.
DR Ensembl; ENSPMET00000034103.1; ENSPMEP00000018189.1; ENSPMEG00000021159.1.
DR GeneID; 106914732; -.
DR KEGG; pmei:106914732; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU362120};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120}; NADP {ECO:0000256|RuleBase:RU362120};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362120}.
FT DOMAIN 33..208
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 210..501
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 513 AA; 58689 MW; 0676B87B374BA534 CRC64;
MTLPLSRSEV FGELRQELYD DEKFHQSDVH IFIIMGASGD LAKKKIYPTL WWLFKDGLLP
EETYFVGFAR SDLTVDAIRT ACMPFMKVTE TEAERLSAFF ARNTYISGKY ADDASFSKLN
AHMLALPGGP EANRLFYLAL PPTVYHDVTK NIKQHCMSTK GWNRVIVEKP FGHDLQSSEE
LSTHLSSLFS EDQIYRIDHY LGKEMVQNLM VLRFGNRIFG PIWNRDSVAC VVLTFKEPFG
TQGRGGYFND FGIIRDVMQN HLLQMLCLVA MEKPASTSSD DVRDEKVKVL KCIPPVTMSD
VVLGQYVGNP EGEGDAKLGY LDDPTVPKGS TQATFATAVL YVHNERWDGV PFILRCGKAL
NERKAEVRLQ FTDVPGDIFD NKCQRNELVV RVQPNEAIYA KMMSKKPGVY FSPEETELDL
TYKSRYKDVK LPDAYERLIL DVFCGSQMHF VRSDELREAW RIFTPLLHQI DKEKPKPIPY
KYGSRGPSEA DDLVKRVGFR YEGTYKWVNP HKL
//
