ID Q97F10_CLOAB Unreviewed; 324 AA.
AC Q97F10;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE SubName: Full=Possible phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AAK80887.1};
GN OrderedLocusNames=CA_C2945 {ECO:0000313|EMBL:AAK80887.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80887.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK80887.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AE001437; AAK80887.1; -; Genomic_DNA.
DR PIR; D97262; D97262.
DR RefSeq; NP_349547.1; NC_003030.1.
DR RefSeq; WP_010966228.1; NC_003030.1.
DR AlphaFoldDB; Q97F10; -.
DR STRING; 272562.CA_C2945; -.
DR GeneID; 44999433; -.
DR KEGG; cac:CA_C2945; -.
DR PATRIC; fig|272562.8.peg.3129; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR OMA; KHGAWQQ; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR PANTHER; PTHR43761:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 14..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 36088 MW; E77D7012D832D3FF CRC64;
MKIVVLDGYT LNPGDMSWEA FKEIGDLTVY DRTDYTGKEE EKTIERARDA EAILTNKTII
TSKVIEKLPK LKYIGVLATG YNVVDLEFAK KKGIVVTNIP QYSTSSVVQM SMALILEICG
HVGQHNASVK KGDWQNCADF SYLKYPIIEL SGKTIGLVGY GSIGKAMQKA AEALGMKVFV
YTPHPDKKYE NESMKFVSLD TLFKEADVIS LHCPLKDDNK EMINKASIKK MKNGVIIINT
ARGGLINERD LYEALKENKV YAAALDVVSF EPIKEDNPLL KAENCIITPH IAWATSEARQ
RLMNIAVNNL KQFVDGCPIN VVNK
//