ID A8MMA4_ALKOO Unreviewed; 313 AA.
AC A8MMA4;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ABW18271.1};
GN OrderedLocusNames=Clos_0712 {ECO:0000313|EMBL:ABW18271.1};
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW18271.1, ECO:0000313|Proteomes:UP000000269};
RN [1] {ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000853; ABW18271.1; -; Genomic_DNA.
DR RefSeq; WP_012158585.1; NC_009922.1.
DR AlphaFoldDB; A8MMA4; -.
DR STRING; 350688.Clos_0712; -.
DR KEGG; aoe:Clos_0712; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000000269; 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; cd12155; PGDH_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
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:UP000000269}.
FT DOMAIN 8..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..275
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 313 AA; 36079 MW; 05FA53828799D42E CRC64;
MKALFTHNLG EENFDKIRAL GYEVVEMREN EAVYNEDIAD VEVLLCYHPF DTLDISKMKN
LKWIQLFSAG VNQVPADVVL NNNITLTNNR GGYSIPMGEW IVLKTLELYK KSAELYSYQK
EKKWHMNSRL LELYGRTITF IGTGSIAKEG AKRFQGFGTT VIGINTKGNE TEYFNKCYPI
DQLDEVLTYS DVVVLTLPYT DQTHHLINKE RLEKMKKDAA IINVSRGSII NEEHLIAHLK
QGNLLGAALD VFETEPLSVE SPLWEMDNVI VTAHNSWMSE MRDQRRFYTA FENMRRYAKG
EELMNVINLK RGY
//
