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Database: UniProt
Entry: A4FXQ5_METM5
LinkDB: A4FXQ5_METM5
Original site: A4FXQ5_METM5 
ID   A4FXQ5_METM5            Unreviewed;       317 AA.
AC   A4FXQ5;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:ABO34989.1};
GN   OrderedLocusNames=MmarC5_0678 {ECO:0000313|EMBL:ABO34989.1};
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880 {ECO:0000313|EMBL:ABO34989.1, ECO:0000313|Proteomes:UP000000253};
RN   [1] {ECO:0000313|EMBL:ABO34989.1, ECO:0000313|Proteomes:UP000000253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333 {ECO:0000313|Proteomes:UP000000253};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO34989.1; -; Genomic_DNA.
DR   RefSeq; WP_011868443.1; NC_009135.1.
DR   AlphaFoldDB; A4FXQ5; -.
DR   STRING; 402880.MmarC5_0678; -.
DR   GeneID; 4927647; -.
DR   KEGG; mmq:MmarC5_0678; -.
DR   eggNOG; arCOG01755; Archaea.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   OrthoDB; 34275at2157; -.
DR   Proteomes; UP000000253; 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:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          20..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   317 AA;  35108 MW;  69092398BDA68A71 CRC64;
     MKIVVLDGYT MNSGDLSWSN LEKFGELNVY DRTSESEVIE RISDSEIVIT NKVIIGREVF
     EKCKNIKYVG VTATGYNVVD TNLAKEFGVT VTNVPAYSTD SVSQLVFSFI LEYCQNVYKY
     NESVKSGDWV NSKDFSYRKF PIVELAGKNL GIIGFGAIGK KVAEIGNAFG MNVIVNTRTI
     SNTNLNVKFV SKEEIFKNSD FLTLHCPLTD ETKEIINKNT LELMKTSSFL INTGRGGLVN
     EKNLADALNL GNIAGAGLDV LSNEPPKEDN PLINAKNTFI TPHVAWASYE ARNRLMNVTI
     NNVKSFIEGN PINVVNK
//
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