ID Q2RIZ2_MOOTA Unreviewed; 298 AA.
AC Q2RIZ2;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=6-phosphogluconate dehydrogenase (Decarboxylating) {ECO:0000313|EMBL:ABC19597.1};
DE EC=1.1.1.44 {ECO:0000313|EMBL:ABC19597.1};
GN OrderedLocusNames=Moth_1283 {ECO:0000313|EMBL:ABC19597.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19597.1};
RN [1] {ECO:0000313|EMBL:ABC19597.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19597.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP000232; ABC19597.1; -; Genomic_DNA.
DR RefSeq; YP_430140.1; NC_007644.1.
DR AlphaFoldDB; Q2RIZ2; -.
DR SMR; Q2RIZ2; -.
DR STRING; 264732.Moth_1283; -.
DR EnsemblBacteria; ABC19597; ABC19597; Moth_1283.
DR KEGG; mta:Moth_1283; -.
DR PATRIC; fig|264732.11.peg.1376; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_9; -.
DR OrthoDB; 9804542at2; -.
DR BRENDA; 1.1.1.44; 1528.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR NCBIfam; TIGR00872; gnd_rel; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF67; 6-PHOSPHOGLUCONATE DEHYDROGENASE YQEC-RELATED; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Oxidoreductase {ECO:0000313|EMBL:ABC19597.1}.
FT DOMAIN 167..296
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 298 AA; 32365 MW; 7BC1551835278A5D CRC64;
MHIGLVGLGR MGLNLALNML DHGHEVRGYA RTKATVDKAA AQGIKGAYSL EELAGQLKTP
RLVWLMIPAG KAVDEVIEQL APLLAPGDII VDGGNSHYRD TLRRYKFLKE KGIHLVDSGT
SGGVEGARHG ACCMVGAEDE VFAYLEPLFK DITVPGGYLH TGPPGSGHYV KMVHNGIEYG
MMQAIGEGME VLAGAPFKLD LKEVARVWRH GSVIRGWLMD LMEKALAKDN TLDGIKDIAY
SSGEGLWTIE EALRLKVPAP VITAALLMRY RSEQEESFAT KVVAALRHEF GGHDVARK
//
