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Database: UniProt
Entry: A0A0W0XLX8_9GAMM
LinkDB: A0A0W0XLX8_9GAMM
Original site: A0A0W0XLX8_9GAMM 
ID   A0A0W0XLX8_9GAMM        Unreviewed;       609 AA.
AC   A0A0W0XLX8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=DlpA protein (Isocitrate and isopropylmalate dehydrogenase family protein) {ECO:0000313|EMBL:KTD45560.1};
GN   Name=dlpA {ECO:0000313|EMBL:KTD45560.1};
GN   ORFNames=Lrub_2357 {ECO:0000313|EMBL:KTD45560.1};
OS   Legionella rubrilucens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=458 {ECO:0000313|EMBL:KTD45560.1, ECO:0000313|Proteomes:UP000054608};
RN   [1] {ECO:0000313|EMBL:KTD45560.1, ECO:0000313|Proteomes:UP000054608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD45560.1,
RC   ECO:0000313|Proteomes:UP000054608};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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:KTD45560.1}.
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DR   EMBL; LNYT01000022; KTD45560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0XLX8; -.
DR   STRING; 458.Lrub_2357; -.
DR   PATRIC; fig|458.5.peg.2460; -.
DR   OrthoDB; 9812532at2; -.
DR   Proteomes; UP000054608; 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   CDD; cd16841; RraA_family; 1.
DR   Gene3D; 1.20.5.3070; -; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   Gene3D; 3.50.30.40; Ribonuclease E inhibitor RraA/RraA-like; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR005493; RraA/RraA-like.
DR   InterPro; IPR036704; RraA/RraA-like_sf.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   Pfam; PF03737; RraA-like; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF89562; RraA-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054608}.
FT   DOMAIN          8..362
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   609 AA;  67334 MW;  3157B896CF137ED7 CRC64;
     MTMNDVIKIA VLPGDGIGEE VTEAALPIVK ALNLPMEIHR GDIGWACWQE QGDPLPEKTW
     QLIRHCDATL IGAITSKPVR EALRELSPKL QKNHLEYVSP LIQLRQKLDL FANVRPCFNL
     VDREQPFHFC IIRENTEGLY AGFDFHPPPE PISQLIRQQK RWQHTSSQDL SVSLRLQSRQ
     GLQRLFEFAF QYAKDNQFAR VTFADKPNVL RQSGAFARDI FEAVAARYSA IHADIANIDA
     AALWLVRRPE EFGVIVAENM FGDILSDVGA AVMGGLGFAP SANMGHQGCY FEPVHGSGPR
     ITSHRANPSA MFLTIGLLLK HFGYNSEAER ITRAIAAVIK DGRYLTYDLG GKSTTEEMAQ
     VIIEQVIHPD LPTPVFLKQR SDAKRLTLDL QLQQLKQYST AEIADALDAC GVDGALLHIK
     PLTSGIKLAG PAYTVQYSPY QRIGQAFKQA ANYIDNVPAN AVIVIDNQGR IDCTVWGDIL
     TQAALVKGIA GTVVNGAVRD VAKILNSNYP LFSVERFMRS GKNRVQKSGE QCPVSINGVT
     IQPGDILFGD DNGVLVIPAD LLAEVLAKAQ AICETENKII DAVKKGQRLD QAREDYRYDQ
     PWLNSSDKG
//
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