ID Q5WZ75_LEGPL Unreviewed; 596 AA.
AC Q5WZ75;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Oxaloacetate decarboxylase alpha-chain {ECO:0000313|EMBL:CAH14737.1};
GN Name=dcoA {ECO:0000313|EMBL:CAH14737.1};
GN OrderedLocusNames=lpl0507 {ECO:0000313|EMBL:CAH14737.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH14737.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH14737.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH14737.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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DR EMBL; CR628337; CAH14737.1; -; Genomic_DNA.
DR RefSeq; WP_011214715.1; NC_006369.1.
DR AlphaFoldDB; Q5WZ75; -.
DR KEGG; lpf:lpl0507; -.
DR LegioList; lpl0507; -.
DR HOGENOM; CLU_000395_4_2_6; -.
DR OMA; EAGMISQ; -.
DR Proteomes; UP000002517; Chromosome.
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}.
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 525..594
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 596 AA; 65684 MW; 8A722A26066DE4A4 CRC64;
MSKTFITDVT LRDAHQCLIA TRMRTEDMLP ICNKMDDVGF WAMEVWGGAT FDACLRFLKE
DPWSRLRQLR QALPNTQLSM LLRGQNLLGY RNYADDVVRA FVKLAVNNGV DVFRVFDALN
DARNLKVAID AIKSHKKHAQ GAICYTTSPV HTLDNFLELG KKLAEMGCDS IAIKDMAGLL
TPAVTVELYA GLKQATGLPV HLHSHSTSGL ASICHYEAVL SGCNHIDTAI SSFSGGASHP
PTEALVAALT DTPYDTELDL NILLEIDDYF KAVRKKYSQF ESEAQNIDPR VQLYQVPGGM
ISNLYNQLRE QNALDKMDAV HKEIPRVRKD LGYPPLVTPT SQIVGTQAVI NVLTGERYKT
ITNEVKLYCQ GKYGTPPGKI SSALRKKAIG RTEVIEVRPG DLLPNELDQL QNEISDLALS
DEDVLLYAMF PEIGRQFLEQ RKNNQLIPEP LLTQSSAPDN SVMSEFDIIL HGESYHVKVA
GYGMIEHGQQ SCFLWVDGVP EEVVVQHSEL HDKIERSSVN NKIGPGDITV AIPGSIIAIH
VSSGDEVKAG QAVLVIEAMK METEIKAPAN GVVAEILCQK GDKVTPGQVL IRVEVS
//