ID A0A0F4PX70_9GAMM Unreviewed; 326 AA.
AC A0A0F4PX70;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KJY99704.1};
GN ORFNames=TW72_08620 {ECO:0000313|EMBL:KJY99704.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY99704.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY99704.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY99704.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY99704.1}.
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DR EMBL; JXXZ01000007; KJY99704.1; -; Genomic_DNA.
DR RefSeq; WP_045978362.1; NZ_PNCF01000011.1.
DR AlphaFoldDB; A0A0F4PX70; -.
DR GeneID; 58228552; -.
DR PATRIC; fig|151081.8.peg.463; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000033664; Unassembled WGS sequence.
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; cd12183; LDH_like_2; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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; 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:UP000033664}.
FT DOMAIN 5..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35935 MW; F140626914D9DE80 CRC64;
MKLALFSSQR YEQHAFSEHC PDNVEVHFFD AQLNELTASL ARGCDSVCVF VNDVVNKQVL
DKLNELGIKL VLLRCAGFNN VDLDHAARLG IEVARVPAYS PEAVAEHCLA LILTLSRKTH
KAYNRVREDN FDLNGLLGFN LHGKTVGLIG CGKIGLALCR ILNGFGAKVL VVDPAKPEGD
FTLVDKATLL AQSDIISLHC PLTEQTHHII NSDALSHMKR GAMLINTGRG ALLDTKACIN
ALKSGQLGYL GLDVYEQESE LFFKDRSEEI LQDDVFARLL TFQNVLITGH QGFFTKEALQ
QIVQTTFDNL LQYAKGEALT NRVCAP
//
