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Database: UniProt
Entry: A0A1S8FHM7_9BURK
LinkDB: A0A1S8FHM7_9BURK
Original site: A0A1S8FHM7_9BURK 
ID   A0A1S8FHM7_9BURK        Unreviewed;       339 AA.
AC   A0A1S8FHM7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OOG42279.1};
GN   ORFNames=B0B52_10795 {ECO:0000313|EMBL:OOG42279.1};
OS   Polaromonas sp. A23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG42279.1, ECO:0000313|Proteomes:UP000218978};
RN   [1] {ECO:0000313|EMBL:OOG42279.1, ECO:0000313|Proteomes:UP000218978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A23 {ECO:0000313|EMBL:OOG42279.1,
RC   ECO:0000313|Proteomes:UP000218978};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {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:OOG42279.1}.
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DR   EMBL; MUNO01000019; OOG42279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8FHM7; -.
DR   STRING; 1944133.B0B52_10795; -.
DR   OrthoDB; 9147650at2; -.
DR   Proteomes; UP000218978; 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   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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218978}.
FT   DOMAIN          3..302
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          126..279
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   339 AA;  37256 MW;  BBE86952F33CCEBD CRC64;
     MDILLLDALV PEAMAWLETR HGVEYRPELA DDMGVLRKAA YKSRGIVFPR QTVVTREFLD
     FMPKLKAVGR LHVGTDNTDL EACKERGIKV IHASSANVRS NAEYLLSSLL LLYRRGVVSA
     LMGKRHPSTQ MGRELHGSTV GILGLAPTAH TLAGMLTGLG VRLIGYDPAV HHTAPIWERL
     RIQPVTLTEL VSQSAAVSVQ MLYAARFRSF VNDKLLAACK HGQLWVGISR SALFDETALA
     AALCDGRIEA CILDGAEDNF TREGSPVQGL KNLFITPRLG SHTREARLRS SWYVAHRMHE
     AITAEQRGVG YVPSSAPMDL ELPGAVSPSQ WSEPEFIAR
//
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