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Database: UniProt
Entry: A0A0G3XLZ6_9SPHN
LinkDB: A0A0G3XLZ6_9SPHN
Original site: A0A0G3XLZ6_9SPHN 
ID   A0A0G3XLZ6_9SPHN        Unreviewed;       487 AA.
AC   A0A0G3XLZ6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966};
DE            Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966};
DE            EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966};
GN   Name=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN   ORFNames=AB433_02925 {ECO:0000313|EMBL:AKM11488.1};
OS   Croceicoccus naphthovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM11488.1, ECO:0000313|Proteomes:UP000035287};
RN   [1] {ECO:0000313|EMBL:AKM11488.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PQ-2 {ECO:0000313|EMBL:AKM11488.1};
RA   Zeng Y., Huang Y.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC       phosphogluconolactone. {ECO:0000256|HAMAP-Rule:MF_00966}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00966};
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|HAMAP-Rule:MF_00966}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
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DR   EMBL; CP011770; AKM11488.1; -; Genomic_DNA.
DR   RefSeq; WP_047823174.1; NZ_JACIEL010000009.1.
DR   AlphaFoldDB; A0A0G3XLZ6; -.
DR   STRING; 1348774.AB433_02925; -.
DR   KEGG; cna:AB433_02925; -.
DR   PATRIC; fig|1348774.3.peg.615; -.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000035287; Chromosome.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
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|HAMAP-Rule:MF_00966};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP-
KW   Rule:MF_00966}; NADP {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00966}; Reference proteome {ECO:0000313|Proteomes:UP000035287}.
FT   DOMAIN          10..189
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          191..486
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         46
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         150
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT                   ECO:0000256|PROSITE-ProRule:PRU10005"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   487 AA;  53481 MW;  DDF9B052E704D495 CRC64;
     MTFSASKLLL FGATGDLSQR MLLPSLCALT SDGLLPANIE VIGTARSEHT DESFRNFAAA
     ALEKFLPSGR QIEIDPFLSR LRYQDLDAST PEGFDALAKC VGLVGTNEDE GLSIFLSTAP
     SLFEPTIKGL AANGLAPNET GGNVRIGLEK PLGTDLATSC QINDAVAGAF PENRIFRIDH
     YLGKETVQNL LALRFANILF EPLWNAAHID HVQITVAETV GLESRAGYYD GSGALRDMVQ
     NHMLQLLALV AMEPPTSFDA TAVRDEKVKV LRALRHVAAN ETVTGQYKAG AINGGAVPGY
     DEELGRDSDT ETFVAIKAHI DNWRWKGVPF YLRTGKRLPE RTTEIIVKFR NVPFSIFEGR
     GAKTLPNTLV IGIQPRENIR LSLMAKVPGL DRGGIRLRQV PLDIAMPDAF AGPERRIAYE
     RLLLDLVEGD QTLFVRRDEV EAQWHWIDAI RETWAEEGMT PKTYTAGSWG PSASIALAER
     DGVTWHE
//
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