(data stored in ACNUC29543 zone)

SWISSPROT: B2JKW8_PARP8

ID   B2JKW8_PARP8            Unreviewed;       479 AA.
AC   B2JKW8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   16-JAN-2019, entry version 64.
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   OrderedLocusNames=Bphy_3342 {ECO:0000313|EMBL:ACC72497.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72497.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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-
CC         1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00966};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001044; ACC72497.1; -; Genomic_DNA.
DR   STRING; 391038.Bphy_3342; -.
DR   EnsemblBacteria; ACC72497; ACC72497; Bphy_3342.
DR   KEGG; bph:Bphy_3342; -.
DR   eggNOG; ENOG4105D8W; Bacteria.
DR   eggNOG; COG0364; LUCA.
DR   HOGENOM; HOG000046191; -.
DR   KO; K00036; -.
DR   OMA; ESLWERS; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000001192; Chromosome 2.
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   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   PANTHER; PTHR23429; PTHR23429; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JKW8.
DR   SWISS-2DPAGE; B2JKW8.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Glucose metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966,
KW   ECO:0000313|EMBL:ACC72497.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN        2    175       G6PD_N. {ECO:0000259|Pfam:PF00479}.
FT   DOMAIN      177    475       G6PD_C. {ECO:0000259|Pfam:PF02781}.
FT   NP_BIND      82     83       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   ACT_SITE    228    228       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING      39     39       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     136    136       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     166    166       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966, ECO:0000256|PROSITE-ProRule:
FT                                PRU10005}.
FT   BINDING     204    204       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     328    328       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     333    333       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
SQ   SEQUENCE   479 AA;  54175 MW;  44A1021B1AF71B91 CRC64;
     MIIFGGAGDL SARKLLPALY MAHTHGNLPA ETRILAIGRR EWQRDDYLKW MEEQSRPFIE
     SSAFDSSAWD RFLSLFEYVR VDVDQPEAYQ RLAEASRQNA LRVFYLSTSP ELFTTICDNL
     SSHGLLDEYS RVVLEKPLGH NLESAKAIND SVGKHFAEHQ IYRIDHYLGK ETVQNLMVLR
     FGNAIFGPLW QAPYIRSVQI TVAESVGVGT RAGFYDHTGA MRDMVQNHLL QLLCIVAMEP
     PVSLDADAVR DEKLKVLRSL RPMTAEDIAR DTVRGQYTAG AVGGEPVKGY LEEANVPPDS
     RAETFVALRA HINNWRWANV PFYLRTGKRM AKKLSEIVIE FADLPFSIMP NSPCGPRNCG
     NRLVIQLQPN ESIQLQMLAK EPGSGMRTLP VNLNLDLEQA FTSRRAEAYE RLLIDVVRGR
     LTHFMRRDEL EAAWTWVDPI IEAWKRNGDK PRAYTAGTFG PGASTAMMAR DNMVWSEES
//

If you have problems or comments...

PBIL Back to PBIL home page