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
//