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Database: UniProt
Entry: U5S1I0_9CLOT
LinkDB: U5S1I0_9CLOT
Original site: U5S1I0_9CLOT 
ID   U5S1I0_9CLOT            Unreviewed;       298 AA.
AC   U5S1I0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Decarboxylating 6-phosphogluconate dehydrogenase {ECO:0000313|EMBL:AGY77453.1};
GN   Name=gnd {ECO:0000313|EMBL:AGY77453.1};
GN   ORFNames=CAETHG_3250 {ECO:0000313|EMBL:AGY77453.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY77453.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY77453.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY77453.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT   systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419}.
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DR   EMBL; CP006763; AGY77453.1; -; Genomic_DNA.
DR   RefSeq; WP_023163071.1; NZ_CP012395.1.
DR   AlphaFoldDB; U5S1I0; -.
DR   KEGG; cah:CAETHG_3250; -.
DR   PATRIC; fig|1341692.11.peg.3262; -.
DR   HOGENOM; CLU_024540_0_0_9; -.
DR   Proteomes; UP000017590; Chromosome.
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}.
FT   DOMAIN          167..296
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
SQ   SEQUENCE   298 AA;  33195 MW;  6EC0851D629B0480 CRC64;
     MDVGLIGLGK MGYNLALNMK EHGHDVTAYD CNEQNVKEAE KDGLAGAYSV EELVSKLKGR
     KVVWLMVPAG KPVDTLIDDL LPLLNKHDII IDGGNSHYKD TLRRYEKIKL KEIDFVDVGT
     SGGIEGARYG ACTMIGAQDE VFEYIEPLIK DISVENGYLH TGENGSGHFV KMVHNGIEYG
     MLEAIGEGFE VLEKSQFNFD FKEIARVWNY GSVIRGWLMQ LMEDAFKNDP KLSSIKGIIH
     SNGEGLWTVQ EALELKVSAP VITESLFTRF RSEEDDTFTG KVIAALRNEF GGHDVEKE
//
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