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Database: UniProt
Entry: L0WAY6_9GAMM
LinkDB: L0WAY6_9GAMM
Original site: L0WAY6_9GAMM 
ID   L0WAY6_9GAMM            Unreviewed;       389 AA.
AC   L0WAY6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Tartrate dehydrogenase {ECO:0000313|EMBL:EKF74136.1};
GN   ORFNames=A11A3_09967 {ECO:0000313|EMBL:EKF74136.1};
OS   Alcanivorax hongdengensis A-11-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF74136.1, ECO:0000313|Proteomes:UP000010164};
RN   [1] {ECO:0000313|EMBL:EKF74136.1, ECO:0000313|Proteomes:UP000010164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-11-3 {ECO:0000313|EMBL:EKF74136.1,
RC   ECO:0000313|Proteomes:UP000010164};
RX   PubMed=23209226; DOI=10.1128/JB.01849-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT   hongdengensis Type Strain A-11-3.";
RL   J. Bacteriol. 194:6972-6972(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EKF74136.1}.
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DR   EMBL; AMRJ01000014; EKF74136.1; -; Genomic_DNA.
DR   RefSeq; WP_008929171.1; NZ_AMRJ01000014.1.
DR   AlphaFoldDB; L0WAY6; -.
DR   STRING; 1177179.A11A3_09967; -.
DR   PATRIC; fig|1177179.3.peg.1983; -.
DR   eggNOG; COG0473; Bacteria.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000010164; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   4: Predicted;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT   DOMAIN          7..370
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   REGION          355..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  43003 MW;  4A3420DC4D1F8173 CRC64;
     METRHARLAL LAGDGIGPEV MAVTDAILAT LIRQHQLPVE VDNLPWPSHQ WHQQHGEMMP
     ADAVRTLRGY DGLLLGALGD PGPLDDPQRY LLSDSVSLAP LLTLRKELDL WACERPARWL
     PGTPCYLADP RARDVDMLVI RENSEGEYTG QGGRLRRGTA DEVATQVEVF TAAATERLIR
     HAFERARQRA ADRTEPRRFR GDKAAQVCLI TKRNAQPHWG DLYTETFQRL AADYPEVDTH
     HELVDAACMK FVQCPWHFDV VVASNLHGDI LTDLAAVLCG GPGLAPSANL NPQDDTIPAL
     FEPVHGSAPD IAGQDLADPR ATLLSLAMLL DWLGPRWPAC QKAAQHLHDT VKADLADSDH
     HHTRATGERL NERLQSAPAT TPERTRRSS
//
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