ID   A0A246G602_9PSED        Unreviewed;       602 AA.
AC   A0A246G602;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Oxaloacetate decarboxylase subunit alpha {ECO:0000313|EMBL:OWP73642.1};
GN   Name=oadA {ECO:0000313|EMBL:OWP73642.1};
GN   ORFNames=CEC48_00710 {ECO:0000313|EMBL:OWP73642.1};
OS   Pseudomonas sp. K2I15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2013577 {ECO:0000313|EMBL:OWP73642.1, ECO:0000313|Proteomes:UP000197956};
RN   [1] {ECO:0000313|EMBL:OWP73642.1, ECO:0000313|Proteomes:UP000197956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2I15 {ECO:0000313|EMBL:OWP73642.1,
RC   ECO:0000313|Proteomes:UP000197956};
RA   Orellana P., Castillo D., Corsini G.;
RT   "Draft genome sequence of the Chilean Antartic Pseudomonas sp. strain
RT   K2I15.";
RL   Submitted (JUN-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:OWP73642.1}.
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DR   EMBL; NIXO01000001; OWP73642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246G602; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000197956; 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;  65615 MW;  9ABB61C18041D012 CRC64;
     MTKKIFVTDT ILRDAHQSLL ATRMRTDDML PICDKLDKVG YWSLEVWGGA TFDACVRFLK
     EDPWERLRKL RAALPNTRLQ MLLRGQNLLG YRHYSDDVVK AFVAKAAVNG IDVFRIFDAM
     NDVRNLRVAI EAVKAAGKHA QGTIAYTTSP VHTVEAFVAQ AKQLESMGCD SIAIKDMAGL
     LTPYATGELV KALKAEQSLP IFIHSHDTAG LAAMCQLKAI ENGADHIDTA ISSFAWGTSH
     PGTESMVAAL KGSEFDTGLS LELLQEIGLY FYAVRKKYHQ FESEFTAVDT RVQVNQVPGG
     MISNLANQLK EQGALNRMNE VLAEIPRVRE DLGFPPLVTP TSQIVGTQAF FNVLAGERYK
     TITNEVKLYL QGGYGKAPGV VNEKLRRQAI GNEEVIDVRP ADLLKPEMTK LRGEIGALAK
     SEEDVLTYAM FPDIGRKFLE ERDAGTLSPE VLLPIPEAGG VARAGGEGVP TEFVIDVHGE
     SYRVDITGVG VKAEGKRHFY LSIDGMPEEV VFEPLNEFVS SGGSKRKHAT EPGHVSTAMP
     GNIVDVLVKE GDVVKAGQAV LITEAMKMET EVQAAIAGKV TAVHVAKGDR VNPGEILIEI
     EG
//