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
//