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Database: UniProt
Entry: R7WKI8_9NOCA
LinkDB: R7WKI8_9NOCA
Original site: R7WKI8_9NOCA 
ID   R7WKI8_9NOCA            Unreviewed;       524 AA.
AC   R7WKI8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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   ORFNames=Rrhod_2875 {ECO:0000313|EMBL:EOM75802.1};
OS   Rhodococcus rhodnii LMG 5362.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM75802.1, ECO:0000313|Proteomes:UP000013525};
RN   [1] {ECO:0000313|EMBL:EOM75802.1, ECO:0000313|Proteomes:UP000013525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM75802.1,
RC   ECO:0000313|Proteomes:UP000013525};
RX   PubMed=23788540;
RA   Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA   Dyson P.J., Facey P.D.;
RT   "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT   Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT   Vector of Trypanosoma cruzi.";
RL   Genome Announc. 1:e00329-13(2013).
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   -!- 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:EOM75802.1}.
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DR   EMBL; APMY01000082; EOM75802.1; -; Genomic_DNA.
DR   RefSeq; WP_010838919.1; NZ_APMY01000082.1.
DR   AlphaFoldDB; R7WKI8; -.
DR   STRING; 38312.GCA_000720375_05702; -.
DR   PATRIC; fig|1273125.3.peg.2745; -.
DR   eggNOG; COG0364; Bacteria.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000013525; 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   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:UP000013525}.
FT   DOMAIN          42..225
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          227..522
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966,
FT                   ECO:0000256|PROSITE-ProRule:PRU10005"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   524 AA;  58304 MW;  C8349438E5EBD780 CRC64;
     MSGAHRHPAS PSDGPRTARP VNPLRDARDK RLPRVAGPGA LVIFGVTGDL ARRKLMPAIY
     DLANRGLLPP GFALVGFARR EWEDDDFAKI VHDAVRAHAR TPFREDVWER LADGLRFVQG
     NFDDPDAYRR LADTLGTLDR ERGTGGNHGF YLAIPPTLFP VVLEQLSRTG LADATDDRWS
     RVVIEKPFGH DLGSARELNA LVNSVFPEDA VFRIDHYLGK ETVQNILALR FANQLFDPLW
     NAHYVDHVQI TMAEDIGLGG RAGYYDGIGA ARDVIQNHLL QLLAFTAMEE PISFEPTELQ
     AEKIKVLRST RPVEPFDTTT ARGQYAAGWQ GGLPVVGLLE EEGFAADSTT ETFAAITVEV
     DTRRWAGVPF YLRTGKRLGR RVTEIAIVFK RAPHLPFDQT MTEELGQNAL VIRIQPDEGV
     TLRFGSKVPG SGMEVRDVTM DFSYGQAFTT TSPEAYERLI LDMLLGEPSL FPGNEEVELS
     WSILDPVLEH WARAGRPQPY EAGTWGPSSA DEMLARAGRE WRRP
//
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