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
//