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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//