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Database: UniProt
Entry: A0A1T0CTQ1_9GAMM
LinkDB: A0A1T0CTQ1_9GAMM
Original site: A0A1T0CTQ1_9GAMM 
ID   A0A1T0CTQ1_9GAMM        Unreviewed;       314 AA.
AC   A0A1T0CTQ1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OOS25501.1};
GN   ORFNames=B0680_01310 {ECO:0000313|EMBL:OOS25501.1};
OS   Moraxella pluranimalium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=470453 {ECO:0000313|EMBL:OOS25501.1, ECO:0000313|Proteomes:UP000189800};
RN   [1] {ECO:0000313|EMBL:OOS25501.1, ECO:0000313|Proteomes:UP000189800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 54913 {ECO:0000313|EMBL:OOS25501.1,
RC   ECO:0000313|Proteomes:UP000189800};
RA   Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA   Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA   Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome sequence of Moraxella pluranimalium CCUG 54913T type
RT   strain.";
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:OOS25501.1}.
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DR   EMBL; MUYU01000006; OOS25501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T0CTQ1; -.
DR   STRING; 470453.B0680_01310; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000189800; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000189800}.
FT   DOMAIN          15..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   314 AA;  34525 MW;  74D5C17C0B7EF8E7 CRC64;
     MKAVFLDRAT FSAQVSLLTP DGISDYQIYD ATPNDTATII ERCQDADIII TNKVLITRDV
     ISALPKLKLI QLTATGMNNV DKTACDEHDV QLYNVAGYSV ASVPEHTFGL MLSAMRALNH
     YHRVATDGTW QADGRFCLLD EPIYDLAGRT LGIIGSGNIG RRVGEIARVF GMTVLYAERQ
     GKSPRNADYT DFDTVLADSD IISLHCPLTD DTLRLINDNT IAKMTKRPLI VNVARGAVVD
     GDSIVKALNQ QQILGYASDV FDDEPFANDD ALLGIKDHPR VLFTPHNAWG SLGAQAKLWQ
     ILSRQVSTFI RQSV
//
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