G6PD2_MYCTO
ID G6PD2_MYCTO Reviewed; 514 AA.
AC P9WN72; L0T6P1; O08407; P0A584;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00966};
DE Short=G6PD 2 {ECO:0000255|HAMAP-Rule:MF_00966};
DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
GN Name=zwf2 {ECO:0000255|HAMAP-Rule:MF_00966}; Synonyms=zwf;
GN OrderedLocusNames=MT1494;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00966}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|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; AE000516; AAK45757.1; -; Genomic_DNA.
DR PIR; B70917; B70917.
DR RefSeq; WP_003407443.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN72; -.
DR SMR; P9WN72; -.
DR EnsemblBacteria; AAK45757; AAK45757; MT1494.
DR KEGG; mtc:MT1494; -.
DR PATRIC; fig|83331.31.peg.1606; -.
DR HOGENOM; CLU_013524_5_0_11; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001020; 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;
KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase.
FT CHAIN 1..514
FT /note="Glucose-6-phosphate 1-dehydrogenase 2"
FT /id="PRO_0000427177"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 69
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 514 AA; 57343 MW; 22A9CCEDC9AB062F CRC64;
MKPAHAAASW RNPLRDKRDK RLPRIAGPCG MVIFGVTGDL ARKKVMPAVY DLANRGLLPP
TFSLVGFARR DWSTQDFGQV VYNAVQEHCR TPFRQQNWDR LAEGFRFVPG TFDDDDAFAQ
LAETLEKLDA ERGTGGNHAF YLAIPPKSFP VVCEQLHKSG LARPQGDRWS RVVIEKPFGH
DLASARELNK AVNAVFPEEA VFRIDHYLGK ETVQNILALR FANQLFDPIW NAHYVDHVQI
TMAEDIGLGG RAGYYDGIGA ARDVIQNHLM QLLALTAMEE PVSFHPAALQ AEKIKVLSAT
RLAEPLDQTT SRGQYAAGWQ GGEKVVGLLD EEGFAEDSTT ETFAAITLEV DTRRWAGVPF
YLRTGKRLGR RVTEIALVFR RAPHLPFDAT MTDELGTNAM VIRVQPDEGV TLRFGSKVPG
TAMEVRDVNM DFSYGSAFAE DSPEAYERLI LDVLLGEPSL FPVNAEVELA WEILDPALEH
WAAHGTPDAY EAGTWGPESS LEMLRRTGRE WRRP
