ID A0A1V9V093_9PSED Unreviewed; 602 AA.
AC A0A1V9V093;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Oxaloacetate decarboxylase subunit alpha {ECO:0000313|EMBL:OQR35583.1};
GN ORFNames=BWR59_05680 {ECO:0000313|EMBL:OQR35583.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR35583.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR35583.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR35583.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OQR35583.1}.
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DR EMBL; MUIN01000003; OQR35583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9V093; -.
DR STRING; 1943632.BWR59_05680; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000192462; Unassembled WGS sequence.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 526..601
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 602 AA; 65601 MW; B9D25A7E88749EBE CRC64;
MSKKIFVTDT ILRDAHQSLL ATRMRTEDML PICEKLDKVG YWSLECWGGA TFDACVRFLK
EDPWERLRQL RAALPNTRLQ MLLRGQNLLG YRHYSDDVVK AFVAKAAVNG IDVFRIFDAM
NDVRNLRVAI EAVKASGKHA QGTIAYTTSP VHTIEAFVAQ AKQMEAMGCD SVAIKDMAGL
LTPYATGELV KALKSEQSLP VFIHSHDTAG LAAMCQMKAI ENGADHIDTA ISSFAWGTSH
PGTESMVAAL KGSEFDTGLD LELLQEIGLY FYAVRKKYHQ FESEFTAVDT RVQVNQVPGG
MISNLANQLK EQGALNRMGE VLAEIPRVRK DLGYPPLVTP TSQIVGTQAF FNVLAGERYK
TITNEVKLYL TGGYGKAPGQ VDEKLRRQAI GNEELIDVRP ADLLKPEMTK LRGEIGALAK
SEEDVLTYAM FPDIGRKFLE ERAAGTLSPE PLLPIPEPGT VAKAGGEGVP TEFVIDVHGE
SYRVDITGVG VKAEGKRHFY LSIDGMPEEV VFEPLNEFVG GGIGKRAQAS KPGHVSTTMP
GNIVDVLVKE GDMVKAGQAV LITEAMKMET EVQAAVAGKV VAIHVAKGDR VNPGEILVEI
EG
//