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Database: UniProt
Entry: A0A1Y6HMC2_9XANT
LinkDB: A0A1Y6HMC2_9XANT
Original site: A0A1Y6HMC2_9XANT 
ID   A0A1Y6HMC2_9XANT        Unreviewed;       476 AA.
AC   A0A1Y6HMC2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ECO:0000313|EMBL:SMR03701.1};
GN   ORFNames=PD5205_02407 {ECO:0000313|EMBL:SMR03701.1};
OS   Xanthomonas fragariae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR03701.1, ECO:0000313|Proteomes:UP000195953};
RN   [1] {ECO:0000313|EMBL:SMR03701.1, ECO:0000313|Proteomes:UP000195953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD5205 {ECO:0000313|EMBL:SMR03701.1};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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|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; LT853885; SMR03701.1; -; Genomic_DNA.
DR   RefSeq; WP_002802225.1; NZ_ORZZ01000146.1.
DR   AlphaFoldDB; A0A1Y6HMC2; -.
DR   STRING; 48664.BER92_11585; -.
DR   KEGG; xfr:BER92_11585; -.
DR   eggNOG; COG0364; Bacteria.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000195953; Chromosome 1.
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; 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.
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|HAMAP-Rule:MF_00966,
KW   ECO:0000313|EMBL:SMR03701.1}.
FT   DOMAIN          6..176
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          179..465
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   REGION          457..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         84..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         137
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   476 AA;  53003 MW;  9C660AE54AB7D92B CRC64;
     MHNTLILFGA TGDLAQRYLF PSLLRLFVDG LLPEDFRIRA LALSPHDTEA FREVLRPRLT
     DALPIAAPEQ IETLLQRVDY RSVDLRDAES VANAVRELAS RHCVSYLAIP PDLYISTCQG
     LALGGALAAP HRLMLEKPIG HDSDSAREIL QLIGALIDED RVFRLDHYLG KAAVQNLIAL
     RFGNTLLEAV WNRTYIESVQ ILVAESEGVD GRDAYYARSG ALRDMVQSHI LQLLCLVAME
     PPASLEADRI RDEKVKVLRS LRPMSAEHAA RDSVRGRYTA GTIDGQPAQA YHPPEGIDVE
     TLVAVTAHID NWRWAGVPFH LCTGKRLAER STRIVVTLKP VTHWLFERPD RQNAVPNRLT
     FQLQPQENIE LGLMSSLAGP EWGAIELQPL ELELSMPTGL HRRIAYERLF VDAFNGNPAL
     FVRDDEVKAA WAWIDSVSNA WKDAQLPLQP YPAGSWGPES ATHFLPPATD AQGNNA
//
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