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Database: UniProt
Entry: E4T6R2_PALPW
LinkDB: E4T6R2_PALPW
Original site: E4T6R2_PALPW 
ID   E4T6R2_PALPW            Unreviewed;       513 AA.
AC   E4T6R2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=Palpr_2270 {ECO:0000313|EMBL:ADQ80406.1};
OS   Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ80406.1, ECO:0000313|Proteomes:UP000008718};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB4;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ80406.1, ECO:0000313|Proteomes:UP000008718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17365 / JCM 13257 / WB4
RC   {ECO:0000313|Proteomes:UP000008718};
RX   PubMed=21475585; DOI=10.4056/sigs.1503846;
RA   Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Paludibacter propionicigenes type strain
RT   (WB4).";
RL   Stand. Genomic Sci. 4:36-44(2011).
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; CP002345; ADQ80406.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4T6R2; -.
DR   STRING; 694427.Palpr_2270; -.
DR   KEGG; ppn:Palpr_2270; -.
DR   eggNOG; COG0364; Bacteria.
DR   HOGENOM; CLU_013524_5_0_10; -.
DR   OMA; VEICVYE; -.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000008718; 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:UP000008718}.
FT   DOMAIN          20..204
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          206..504
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         165
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT                   ECO:0000256|PROSITE-ProRule:PRU10005"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   513 AA;  58802 MW;  15B5E67707B7CB39 CRC64;
     MEEVIKKVTR KNPVESQILV IFGSNGDLAK RKLLPAIFQL YLDNLLPERF AVLGAGSMEK
     TEAENRTDVG ASLLEFATKG ATDNPEKLQL FLENVYYQKV HNETEEDFGL LKQYIDDLSA
     RLELPQNIIY YFSIPPFLYE VVAGHLVKYG LNEEATGWKR IIIEKPFGYS YDTAIDLDKK
     LRNGFNEDQI YRIDHYLGKE TVQNIMVTRF SNGFFEPIWN RKYIDRVEIT ASEKIGVGSR
     GGYYDTSGAM RDMIQNHLLQ VLAVVAMEPP SIFDSESIRN ESVKVLQSLR PIKPAEITQN
     VVRGQYIETL VDDVIQKGYR QEKGVAPNSK TETFVALRVF VDNWRWGDVP FYIRTGKQLP
     EHVTEVTIHL KPAPHQLFKQ RCVAQSTNMI ILRISPDAGV AVDFGMKIPG AGYKVQNVNM
     DFHYSDLAET KISEAYERLL LDCMIGDSTL YARADAVKAS WKFVDPILQA WKTNQDIPLY
     FYECNTWGPK EANLLFGNKE LKWRPPFKKF KTQ
//
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