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Database: UniProt
Entry: V4P0P6_9CAUL
LinkDB: V4P0P6_9CAUL
Original site: V4P0P6_9CAUL 
ID   V4P0P6_9CAUL            Unreviewed;       328 AA.
AC   V4P0P6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ESQ81691.1};
GN   ORFNames=AEAC466_20570 {ECO:0000313|EMBL:ESQ81691.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ81691.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ81691.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ81691.1,
RC   ECO:0000313|Proteomes:UP000017826};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ81691.1}.
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DR   EMBL; AWGE01000026; ESQ81691.1; -; Genomic_DNA.
DR   RefSeq; WP_023460089.1; NZ_AWGE01000026.1.
DR   AlphaFoldDB; V4P0P6; -.
DR   STRING; 1282362.AEAC466_20570; -.
DR   PATRIC; fig|1282362.3.peg.4055; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000017826; 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; cd05301; GDH; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017826}.
FT   DOMAIN          21..323
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..292
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   328 AA;  36237 MW;  8810451A214B1B42 CRC64;
     MNTQKLKVVL TVKLPDAVET RMRELFNTTL WLFMTPMPPD RVLEVARDTD VLVTSINDRI
     DADFFANCGD RLKMIANFGV GHDHIDIAAA TEKGIMVTNT PGVLTEDTAE MTMGLILAVS
     RRFVEGAELV QNGEFSAWSP TFMLGRRIFG KRLGIIGMGR IGQALARRAK AFGMSVHYHN
     RKPVSARISD ELGATYWDDL DQMLSRMDVV SINAPGGTGT QHMLNADRLA RLQPHAILVN
     TARGQIVDEQ ALAAMLRNNR IAGVGLDVYE REPAINPELI GLPNAILLPH MASSTIEARQ
     DMGDRVILNI KTHQDGHRPP DRVIPAML
//
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