ID A0A6A7XXP0_9HYPH Unreviewed; 492 AA. AC A0A6A7XXP0; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 14-DEC-2022, entry version 9. 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:MQT11414.1}; GN ORFNames=F0357_01730 {ECO:0000313|EMBL:MQT11414.1}; OS Segnochrobactrum spirostomi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Segnochrobactraceae; Segnochrobactrum. OX NCBI_TaxID=2608987 {ECO:0000313|EMBL:MQT11414.1, ECO:0000313|Proteomes:UP000332515}; RN [1] {ECO:0000313|EMBL:MQT11414.1, ECO:0000313|Proteomes:UP000332515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sp-1 {ECO:0000313|EMBL:MQT11414.1, RC ECO:0000313|Proteomes:UP000332515}; RA Akter S., Shazib S.U.A., Shin M.K.; RT "Segnochrobactrum spirostomi gen. nov., sp. nov., isolated from the ciliate RT Spirostomum cf. yagiui and description of a novel family, RT Segnochrobactraceae fam. nov. within the order Rhizobiales of the class RT Alphaproteobacteria."; RL Submitted (SEP-2019) 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|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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MQT11414.1}. 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; VWNA01000001; MQT11414.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6A7XXP0; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000332515; Unassembled WGS sequence. 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR TIGRFAMs; TIGR00871; zwf; 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:UP000332515}. FT DOMAIN 14..189 FT /note="G6PD_N" FT /evidence="ECO:0000259|Pfam:PF00479" FT DOMAIN 191..488 FT /note="G6PD_C" FT /evidence="ECO:0000259|Pfam:PF02781" FT ACT_SITE 242 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 17..24 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 51 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 341 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" SQ SEQUENCE 492 AA; 54754 MW; 2EE114E0A3858218 CRC64; MVSRIVEVDP FDIVVFGATG DLSRRKLIPA LYHRDHAGQV PADARIFGTA RRHMTNEEFV ADAKKCVLDH VKATDIETAS LDRFLARLAY VGTDATSAEG WDDLSAALGR DEERVRVYYL ATAPELFGPI CERLASHGLV TSNARLVVEK PIGKNLESAH QVNDQIGKYF PEERVYRIDH YLGKETVQNL MALRFANALF EPLWNSAHID HVQITVAETL GVESRAGYYD TAGALRDMVQ NHILQLLCLV AMEPPTSLGA DAVRDEKLKV LKSLKPVDEA NVDLLTVRGQ YKAGASAGGA VAGYLEELGK PSSETETFVA LKAEINNWRW AGVPFYLRTG KRLASRVSEI VVAFRHIPHS VFDGGAGPIS NNRLVIRLQP DEGVRLWLMI KDPGPGGMRL QYVPLDMSFA EAFGVRNPDA YERLIMDVVR GNQTLFMRRD EVEAAWTWVD PILEAWKSRR EPPKPYVSGT WGPSAAVALI ERDGRTWHED DA //