ID G7MCW4_9CLOT Unreviewed; 325 AA.
AC G7MCW4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:EHI98694.1};
DE EC=1.1.1.215 {ECO:0000313|EMBL:EHI98694.1};
GN ORFNames=CDLVIII_2013 {ECO:0000313|EMBL:EHI98694.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI98694.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI98694.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI98694.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CM001240; EHI98694.1; -; Genomic_DNA.
DR RefSeq; WP_009169372.1; NZ_CM001240.1.
DR AlphaFoldDB; G7MCW4; -.
DR STRING; 641107.CDLVIII_2013; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_9; -.
DR Proteomes; UP000005106; Chromosome.
DR GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:EHI98694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT DOMAIN 7..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 37086 MW; F9AB335B4A0F4F46 CRC64;
MEKPKVFIAM KIPKEVEAYI GEYCEYEIWQ ADRDITKDEL KHKLFDKDGV LLMGIKIDED
LLKYAPRLKV VSNFTVGYNN FDIEIMKKRK VIGTNVPNVM NNSVADLVFG LILSVSRKIT
QLDKYVKNNK WKNSIDKNFY GIDVHQSTLG IIGMGRIGEV VAKRAKFGFD MNVLYHNRNR
RMDLEETLGV EYSDFKDILK KSDFIVLLTP LTEETYHLID FEEFKLMKNT AVFINVSRGQ
TVNETALIDA LKSNKIFGAG LDVYEKEPIS LDNELINMPN VVTLPHIGTA TQKTQFDMAM
VAAKNLVEAV CGKSPENVVK ELRDL
//
