GenomeNet

Database: UniProt
Entry: A0A0F0L3K2_9MICO
LinkDB: A0A0F0L3K2_9MICO
Original site: A0A0F0L3K2_9MICO 
ID   A0A0F0L3K2_9MICO        Unreviewed;       515 AA.
AC   A0A0F0L3K2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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_2 {ECO:0000313|EMBL:KJL27708.1};
GN   Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966};
GN   ORFNames=RS83_02761 {ECO:0000313|EMBL:KJL27708.1};
OS   Microbacterium oxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL27708.1, ECO:0000313|Proteomes:UP000033640};
RN   [1] {ECO:0000313|EMBL:KJL27708.1, ECO:0000313|Proteomes:UP000033640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEL4b {ECO:0000313|EMBL:KJL27708.1,
RC   ECO:0000313|Proteomes:UP000033640};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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|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:KJL27708.1}.
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; JYIW01000026; KJL27708.1; -; Genomic_DNA.
DR   RefSeq; WP_045280085.1; NZ_JYIW01000026.1.
DR   AlphaFoldDB; A0A0F0L3K2; -.
DR   PATRIC; fig|82380.11.peg.2796; -.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000033640; 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}.
FT   DOMAIN          30..215
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          217..513
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         67
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00966"
FT   BINDING         109..110
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   515 AA;  57556 MW;  742CF7E72D4B4449 CRC64;
     MSVPISRGHN PLRDPDDRRL NRIAGPSALV IFGVTGDLSR KKLMPAVYDL ANRGLLPPGF
     ALVGFARRDW EDQDFAKVVY DAVKQHARTP FREETWEQLL QGIRFVSGEF DNPESFVKLR
     ETVDQLDVER GTMGNHAFYL SIPPKSFAVV AQQLKDSGLV GDEEGEDRWR RVVIEKPFGH
     DLESARELNK ALEVAFSADS IFRIDHYLGK ETVQNILALR FANELYEPIW NRNYVDHVQI
     TMAEDIGVGG RAGYYDGVGA ARDVIQNHLL QLLALTAMEE PISLSAEHLR AEKEKVLAAV
     HVPDDLSQAT ARGQYAGGWQ GGEKVTGFLD EEGMNPESAT ETYAAIKLEI DTRRWSGVPF
     YLRTGKRLGR RVTEVAVVFK RAPEHLFGRS NTSELGQNAL VIRVQPDEGV TIRFGSKVPG
     NGTNVRDVTM DFGYGHAFTE ASPEAYERLI LDVLLGDPPL FPRHEEVELS WKILDPVEKF
     WAAEGGPVEQ YAPGSWGPAA ADDLLARDGR VWRRP
//
DBGET integrated database retrieval system