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Database: UniProt
Entry: A8FRW0_SHESH
LinkDB: A8FRW0_SHESH
Original site: A8FRW0_SHESH 
ID   A8FRW0_SHESH            Unreviewed;       323 AA.
AC   A8FRW0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:ABV35583.1};
GN   OrderedLocusNames=Ssed_0972 {ECO:0000313|EMBL:ABV35583.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35583.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35583.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35583.1,
RC   ECO:0000313|Proteomes:UP000002015};
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., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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; CP000821; ABV35583.1; -; Genomic_DNA.
DR   RefSeq; WP_012141319.1; NC_009831.1.
DR   AlphaFoldDB; A8FRW0; -.
DR   STRING; 425104.Ssed_0972; -.
DR   KEGG; sse:Ssed_0972; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_6; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000002015; 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; 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:UP000002015}.
FT   DOMAIN          23..323
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..291
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   323 AA;  34990 MW;  818EE1E9EF284B33 CRC64;
     MNIVVLDGYT LNPGDLDWQP LVKIAKQGRE GQFHCYDRTS EAELISRASG ADIIFTNKTP
     ITAETLSQLP NLKYIGVLAT GTNVVDLNCA RERGVAVTNV PGYGPDAVAQ MVFAHILHHT
     QRVSIHHSAV SEGKWTDCED FCFTLAPLQS LQGKTLGLMG YGAIGRQVAN IALAFGMKVL
     VNTRTEPLDL PPGVKWAAFD SMIPRVDILS LHCPLTEATD KIINRTVLEK MRSSAILINT
     ARGGLIDEAA LKQALDEGEI AAAGVDVLST EPPQADNPLL NAVNISISPH NSWATREARQ
     NLLNIAIGNL QAFLSEKPRN RVN
//
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