ID Q8FT74_COREF Unreviewed; 514 AA. AC Q8FT74; C8NP06; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 127. 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}; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18506.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC18506.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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}. 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; BA000035; BAC18506.1; -; Genomic_DNA. DR RefSeq; WP_006767697.1; NZ_GG700683.1. DR AlphaFoldDB; Q8FT74; -. DR STRING; 196164.gene:10742117; -. DR KEGG; cef:CE1696; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_11; -. DR OrthoDB; 9802739at2; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000001409; 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:UP000001409}. FT DOMAIN 32..215 FT /note="Glucose-6-phosphate dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF00479" FT DOMAIN 217..512 FT /note="Glucose-6-phosphate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02781" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 488..514 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 268 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 69 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 176 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 206 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 210 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966, FT ECO:0000256|PROSITE-ProRule:PRU10005" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 366 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" SQ SEQUENCE 514 AA; 57621 MW; 27CFBFDD591C42B8 CRC64; MSSHTNPTTW INPLRDPQDK RLPRIAGPSG LVIFGVTGDL ARKKLLPAIY DLANRGLLPP GFALVGYGRR DWSKEDFENY VREAVEAGAR TEFRGNVWER LAEGMEFVKG NFDDDSAFDN LADTLKRLDE TRGTAGNWAF YLSIPPDSFA AVCHQLERSG MAASTDESWR RVIIEKPFGN DLKTAHELNE TVNAVFPEES VFRIDHYLGK ETVQNILALR FANQLFEPLW NSNYVDHVQI TMAEDIGLGG RAGYYDGIGA ARDVIQNHLI QLLALVAMEE PISFTPTQLQ AEKIKVLRAT KPSLPIAENS ARGQYSAGWQ GSEYVKGLRE EDGFDPESTT ETYAACTLEI TSRRWAGVPF YLRTGKRLGR RVTEIAVVFK DAPHQPFDPG MTAALGNNAI VIRVQPDEGV LIRFGSKVPG SAMEVRDVNM DFSYSESFTE ESPEAYERLI LDALLDESSL FPTNEEVELS WKILDPILEI WEENGQPEEY PAGTWGPKSA DEMLARNGHQ WRRP //