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Database: UniProt
Entry: A0A0W0Z9X4_LEGSP
LinkDB: A0A0W0Z9X4_LEGSP
Original site: A0A0W0Z9X4_LEGSP 
ID   A0A0W0Z9X4_LEGSP        Unreviewed;       598 AA.
AC   A0A0W0Z9X4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Oxaloacetate decarboxylase subunit alpha {ECO:0000313|EMBL:KTD65912.1};
GN   ORFNames=Lspi_0331 {ECO:0000313|EMBL:KTD65912.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD65912.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD65912.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD65912.1,
RC   ECO:0000313|Proteomes:UP000054877};
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   -!- 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:KTD65912.1}.
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DR   EMBL; LNYX01000004; KTD65912.1; -; Genomic_DNA.
DR   RefSeq; WP_058482274.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0Z9X4; -.
DR   STRING; 452.Lspi_0331; -.
DR   PATRIC; fig|452.5.peg.365; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000054877; Unassembled WGS sequence.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005776; OadA.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01108; oadA; 1.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054877}.
FT   DOMAIN          4..264
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          526..595
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   598 AA;  66387 MW;  0689F792D1E9D4EC CRC64;
     MAATHITDVT LRDAHQCLIA TRLRTEDMLP ACKKMDQVGF WAMEVWGGAT FDSCLRFLKE
     DPWQRLHLLR QALPNTRLSM LLRGQNLLGY RHYADDVVKA FVKLAANNGV DVFRVFDALN
     DVRNLRVAIE SVKACKKHAQ GTICYTTSPV HTIENFVDMG KALTDLGCDS IAIKDMAGLL
     TPSDTVNLYQ ALARATQLPI HLHTHATSGL AAICHYQAVL AGCRHIDTAI SSFSGGASHP
     ATEPLVAALA GSEFDTGLDL NLLLEIGDYF HEIRKKYQQF ESEARDIDPR VQLYQVPGGM
     ISNLYNQLKE QQALDKMAAV HEEIPNVRKD LGYPPLVTPT SQVVGTQAVM NVLTGERYKT
     ITNEVKLYCQ GKYGATPGKI NARLRKKAIG RTEVIDVRPA DLLPNELNRL RKEIGDLAES
     EEDVLSYAMF PEIARQFLRE RQSNTLAPEP LLGKQLSDER SKLSEFDITL HGESYHVKVA
     GFGDRERGRQ ACFLWVDEVP EEVIIELPQQ DKGLTDSRPV TKTSGPGDIK VAMPGTIVNV
     FVKTGDKVKI GQVLFVLEAM KMETEIQAPF DGKVTEVYCS KGDKVTPEQV LMQLAGRT
//
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