(data stored in SCRATCH zone)

SWISSPROT: D6ZBX5_SEGRD

ID   D6ZBX5_SEGRD            Unreviewed;       515 AA.
AC   D6ZBX5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 53.
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=Srot_0465 {ECO:0000313|EMBL:ADG96952.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96952.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96952.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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}.
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DR   EMBL; CP001958; ADG96952.1; -; Genomic_DNA.
DR   RefSeq; WP_013137408.1; NC_014168.1.
DR   STRING; 640132.Srot_0465; -.
DR   EnsemblBacteria; ADG96952; ADG96952; Srot_0465.
DR   KEGG; srt:Srot_0465; -.
DR   eggNOG; ENOG4105D8W; Bacteria.
DR   eggNOG; COG0364; LUCA.
DR   HOGENOM; HOG000046191; -.
DR   KO; K00036; -.
DR   OMA; VEICVYE; -.
DR   OrthoDB; 1153269at2; -.
DR   BioCyc; SROT640132:G1GLH-465-MONOMER; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000002247; 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   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; D6ZBX5.
DR   SWISS-2DPAGE; D6ZBX5.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:ADG96952.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN       33    216       G6PD_N. {ECO:0000259|Pfam:PF00479}.
FT   DOMAIN      218    513       G6PD_C. {ECO:0000259|Pfam:PF02781}.
FT   ACT_SITE    269    269       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING      70     70       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     177    177       NADP. {ECO:0000256|HAMAP-Rule:MF_00966}.
FT   BINDING     207    207       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     211    211       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966, ECO:0000256|PROSITE-ProRule:
FT                                PRU10005}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     264    264       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
FT   BINDING     367    367       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00966}.
SQ   SEQUENCE   515 AA;  57164 MW;  C997F1805F1C5905 CRC64;
     MTKAALPPAG WTNPLRDERD KRMPRIAGPC GLVVFGVTGD LSRHKLMPAV YDLANRGLLS
     PSFSLVGFGR RDWDDAGFAD FVRDCVQAKA RTPFREETFA RLAQGMRFVQ GAFDEDASFE
     RIADALRGLD EDRGTGGNYA FYLSVPPKDF PVVFKHLSAT GLAHPPEGSW RRAVVEKPFG
     HDLESAIELN GVIKEVFDER SIFRIDHYLG KETVQNILAL RFANQLFEPI WNAHYVDHVQ
     ITMAEDIGLG GRAGYYDGIG AARDVIQNHL LQLLALVAME EPVSFAAHEV TTEKTKVLSA
     AKLSYPLDET TARGQYARGW QGGQEVCGLL EEEGFASDST TETFAAITVE VDSRRWAGVP
     FYLRTGKRLG RRVTEIALVF KRAPHLPFDE AMTEELGQNA LVIRVQPDEG VTLRFGSKVP
     GSAMRVRDVN MDFNYGQAFT ESSPEAYERL ILDVLLGEPS LFPVTDEVEL SWKILDPVLE
     HWGAGGAPEQ YPSGGWGPKS ATEMLARSGR TWRRP
//

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