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Database: UniProt
Entry: F3FIV7_PSESX
LinkDB: F3FIV7_PSESX
Original site: F3FIV7_PSESX 
ID   F3FIV7_PSESX            Unreviewed;       602 AA.
AC   F3FIV7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:EGH30143.1};
DE            EC=6.4.1.1 {ECO:0000313|EMBL:EGH30143.1};
GN   ORFNames=PSYJA_14672 {ECO:0000313|EMBL:EGH30143.1};
OS   Pseudomonas syringae pv. japonica str. M301072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH30143.1, ECO:0000313|Proteomes:UP000004471};
RN   [1] {ECO:0000313|EMBL:EGH30143.1, ECO:0000313|Proteomes:UP000004471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH30143.1}.
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DR   EMBL; AEAH01000683; EGH30143.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3FIV7; -.
DR   PATRIC; fig|629262.5.peg.2428; -.
DR   HOGENOM; CLU_000395_4_2_6; -.
DR   Proteomes; UP000004471; Unassembled WGS sequence.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
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;
KW   Ligase {ECO:0000313|EMBL:EGH30143.1};
KW   Pyruvate {ECO:0000313|EMBL:EGH30143.1}.
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;  65587 MW;  726F3BDC964FA3B2 CRC64;
     MSKKIFVTDT ILRDAHQSLL ATRMRTEDML PICDKLDQVG YWSLEVWGGA TFDACVRFLK
     EDPWERLRQL RAALPNTRLQ MLLRGQNLLG YRHYSDDVVK AFVAKAAVNG IDVFRIFDAM
     NDVRNLRVAI EAVKAAGKHA QGTIAYTTSP VHTIEAFVAQ ARQMEAMGCD SVAIKDMAGL
     LTPYATGELV KALKAEQSLP VFIHSHDTAG LAAMCQLKAI ESGADHIDTA ISSFAWGTSH
     PGTESMVAAL KGSEFDTGLD LELLQEIGLY FYAVRKKYHQ FESEFTAVDT RVQVNQVPGG
     MISNLANQLK EQGALNRMSE VLAEIPRVRK DLGYPPLVTP TSQIVGTQAF FNVLAGERYK
     TITNEVKLYL QGGYGKAPGQ VDEKLRRQAI GHEEQIDVRP ADLLKPEMTK LRADIGALAK
     SEEDVLTFAM FPDIGRKFLE ERAAGTLAPE VLLPIPEAGS VAKAGGEGVP TEFVIDVHGE
     TYRVDITGVG VKAEGKRHFY LTIDGMPEEV VFEPLNEFVG GGASKRKQAH APGDVSTTMP
     GNIVDVLVKE GDVVKAGQAV LITEAMKMET EVQASVAGKV VAIHVAKGDR VNPGEVLIEI
     EG
//
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