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Database: UniProt
Entry: A0A0S8ZL52_9PSED
LinkDB: A0A0S8ZL52_9PSED
Original site: A0A0S8ZL52_9PSED 
ID   A0A0S8ZL52_9PSED        Unreviewed;       602 AA.
AC   A0A0S8ZL52;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:KQN54024.1};
DE            EC=6.4.1.1 {ECO:0000313|EMBL:KQN54024.1};
GN   ORFNames=ASE98_17815 {ECO:0000313|EMBL:KQN54024.1};
OS   Pseudomonas sp. Leaf48.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN54024.1, ECO:0000313|Proteomes:UP000051774};
RN   [1] {ECO:0000313|EMBL:KQN54024.1, ECO:0000313|Proteomes:UP000051774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf48 {ECO:0000313|EMBL:KQN54024.1,
RC   ECO:0000313|Proteomes:UP000051774};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN54024.1, ECO:0000313|Proteomes:UP000051774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf48 {ECO:0000313|EMBL:KQN54024.1,
RC   ECO:0000313|Proteomes:UP000051774};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQN54024.1}.
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DR   EMBL; LMLH01000004; KQN54024.1; -; Genomic_DNA.
DR   RefSeq; WP_060540228.1; NZ_LMLH01000004.1.
DR   AlphaFoldDB; A0A0S8ZL52; -.
DR   STRING; 1736221.ASE98_17815; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000051774; 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:KQN54024.1};
KW   Pyruvate {ECO:0000313|EMBL:KQN54024.1}.
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;  65417 MW;  361AAC5754067606 CRC64;
     MSKKIYVTDT ILRDAHQSLL ATRMRTEDML PICDKLDKVG YWSLECWGGA TFDACVRFLK
     EDPWERLRQL RAALPNTRLQ MLLRGQNLLG YRHYSDDVVK AFVAKAAVNG IDVFRIFDAM
     NDVRNLRVAI EAVKAAGKHA QGTIAYTTSP VHTIDAFVAQ AKQMEAMGCD SVAIKDMAGL
     LTPYATGELV RALKAEQSLP VFIHSHDTAG LATMCQLKAI ENGADHIDTA ISSFASGTSH
     PGTESMVAAL KGTEFDTGLN LELLQEIGLY FYAVRKKYHQ FESEFTAVDT RVQVNQVPGG
     MISNLANQLK EQGALNRMSE VLAEIPRVRE DLGFPPLVTP TSQIVGTQAF FNVLAGERYK
     TITNEVKLYL QGGYGKAPAP VNEQLRRQAI GSEEVIDVRP ADLLKPEMAK LRADIGALAK
     SEEDVLTYAM FPDIGRKFLE ERAAGTLTPE VLLPIPEAGG VASAGGEGVP TEFVIDVHGE
     TYRVDITGVG VKAEGKRHFY LSIDGMPEEV VFEPLNEFVG GGSSKRKQAT APGHVSTTMP
     GNIVDVLVKE GDTVKAGQAV LITEAMKMET EVQSAIAGKV TAIHVAKGDR VNPGEILIEI
     EG
//
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