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Database: UniProt
Entry: A0A095SLV1_9GAMM
LinkDB: A0A095SLV1_9GAMM
Original site: A0A095SLV1_9GAMM 
ID   A0A095SLV1_9GAMM        Unreviewed;       375 AA.
AC   A0A095SLV1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Tartrate dehydrogenase {ECO:0000313|EMBL:KGD65557.1};
GN   ORFNames=Y5S_01450 {ECO:0000313|EMBL:KGD65557.1};
OS   Alcanivorax nanhaiticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD65557.1, ECO:0000313|Proteomes:UP000029444};
RN   [1] {ECO:0000313|EMBL:KGD65557.1, ECO:0000313|Proteomes:UP000029444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19-m-6 {ECO:0000313|EMBL:KGD65557.1,
RC   ECO:0000313|Proteomes:UP000029444};
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:KGD65557.1}.
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DR   EMBL; ARXV01000004; KGD65557.1; -; Genomic_DNA.
DR   RefSeq; WP_035231754.1; NZ_ARXV01000004.1.
DR   AlphaFoldDB; A0A095SLV1; -.
DR   STRING; 1177154.Y5S_01450; -.
DR   PATRIC; fig|1177154.3.peg.1479; -.
DR   eggNOG; COG0473; Bacteria.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000029444; 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          6..368
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   375 AA;  41046 MW;  C01A510DA2F9C93A CRC64;
     MTQTLKIALL PGDGIGPEVM TVTAEILAGL VSRFQLPVEV QSFAWPSHSW HQQHGQMMPE
     DGVDQLRAFD AILLGALGDP GPIDDPQRYV LSDSISLAPL LALRKELNLW ACERPARWLP
     GAPQYLADSR ANNVDMLVIR ENSEGEYSNQ GGRLRAGTPN EVATQVEVFT AGATERLIRH
     AFDRARQRAA LRHTPRHFAT GKEAQVCLIT KRNAQPFWGD LYTETFARIA REYPDVDTHH
     ELVDAACMKF VQCPWRFDVV VASNLHGDIL TDLAAVLCGG PGLAPSANLN PADARIPALF
     EPVHGSAPDI AGRNMADPRA TLMSLAMLLD YLAHKHPAIG NAAQHLHDLI AEDLKYAFSG
     TRETGQRLSQ RLAAG
//
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