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Database: UniProt
Entry: A0A1G8M1U4_9PSED
LinkDB: A0A1G8M1U4_9PSED
Original site: A0A1G8M1U4_9PSED 
ID   A0A1G8M1U4_9PSED        Unreviewed;       602 AA.
AC   A0A1G8M1U4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:SDI61908.1};
GN   ORFNames=SAMN05216272_11329 {ECO:0000313|EMBL:SDI61908.1};
OS   Pseudomonas panipatensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=428992 {ECO:0000313|EMBL:SDI61908.1, ECO:0000313|Proteomes:UP000199636};
RN   [1] {ECO:0000313|EMBL:SDI61908.1, ECO:0000313|Proteomes:UP000199636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 7469 {ECO:0000313|EMBL:SDI61908.1,
RC   ECO:0000313|Proteomes:UP000199636};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNDS01000013; SDI61908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8M1U4; -.
DR   STRING; 428992.SAMN05216272_11329; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000199636; 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;
KW   Pyruvate {ECO:0000313|EMBL:SDI61908.1}.
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;  65504 MW;  68A5BD1FEB9D99B1 CRC64;
     MSKKVTVTDI ILRDAHQSLL ATRMRTEDML PICDKLDKVG YWSLEVWGGA TFDACVRFLK
     EDPWERLRKL KAALPNTRLQ MLLRGQNLLG YRHYSDDVVR AFVAKAAVNG IDVFRIFDAM
     NDVRNLRVSI EAVKAAGKHA QGTICYTTSP VHTIEAFVAQ GRAMADMGVD SIAIKDMAGL
     LTPYATGELV KALKDALPLD VVVHSHDTAG VASMCQLKAI ENGASRIDTA ISSMAWGTSH
     PGTESMVAAL RGTPYDTGLD LELIQEIGLY FYAVRKKYHQ FESAFTGVDT RVQVNQVPGG
     MISNLANQLK EQGALNRMDE VLAEIPKVRA DLGYPPLVTP TSQIVGTQAF FNVLAGERYK
     TITNEVKLYL QGRYGKAPGE VSEQLRRQAI GSEEVIDVRP ADLIKAELNK LREEIGSLAK
     SEEDVLTYAM FPDIGRKFLE ERAAGTLKPE ELLPIPNGNG VAAAGGEGVP TEFVIDVHGE
     TYRVDITGVG VKGENKRHFY LSIDGMPEEV LFEPLNEYVG GAGNKRKQAS APGHVTTTMP
     GNIVDVLVKE GDSVKAGQAV LITEAMKMET EVQAGIAGTV KAIHVAKGDR VNPGEILIEI
     EG
//
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