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Database: UniProt
Entry: A0A2S5KIM7_9PROT
LinkDB: A0A2S5KIM7_9PROT
Original site: A0A2S5KIM7_9PROT 
ID   A0A2S5KIM7_9PROT        Unreviewed;       315 AA.
AC   A0A2S5KIM7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:PPC74674.1};
GN   ORFNames=C4K68_25515 {ECO:0000313|EMBL:PPC74674.1};
OS   Proteobacteria bacterium 228.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=2083153 {ECO:0000313|EMBL:PPC74674.1, ECO:0000313|Proteomes:UP000238196};
RN   [1] {ECO:0000313|EMBL:PPC74674.1, ECO:0000313|Proteomes:UP000238196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=228 {ECO:0000313|EMBL:PPC74674.1,
RC   ECO:0000313|Proteomes:UP000238196};
RA   Krishnan R., Ramesh Kumar N.;
RT   "novel marine gammaproteobacteria from coastal saline agro ecosystem.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:PPC74674.1}.
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DR   EMBL; PRLP01000143; PPC74674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5KIM7; -.
DR   OrthoDB; 5289001at2; -.
DR   Proteomes; UP000238196; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12169; PGDH_like_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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000238196}.
FT   DOMAIN          25..310
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..283
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   315 AA;  33984 MW;  548C8936C853561E CRC64;
     MKITILDDYQ GIALSMADWS EVHTLAEVRV CRELLTGEAL QAAISDADII CAMRERTLFD
     RAQLQQLPKL KLLITSGMRN AAIDMDAARE LGIVVSGTPN NGAAAAEHTW ALILATVRHI
     PLEDQRIRQG QWQTTVGGDL KGKTLGIVGL GNLGQQVARV AQVFGMKVLA WSPNLTAERA
     AAAGVEYADK QRLLQKSDIV TLHMKLSEST HHLLQADDLA LMPAHGILIN TSRGQLVEEN
     ALIAALSNGQ IAAAGLDVFD QEPIAPDHPL LKLSNTVLTS HVGFVTRETY TLFYQGMVDA
     IVAFCQGAPT KVLNG
//
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