ID W0E0J0_MARPU Unreviewed; 605 AA.
AC W0E0J0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:AHF04395.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:AHF04395.1};
GN ORFNames=MARPU_11480 {ECO:0000313|EMBL:AHF04395.1};
OS Marichromatium purpuratum 984.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF04395.1, ECO:0000313|Proteomes:UP000005275};
RN [1] {ECO:0000313|EMBL:AHF04395.1, ECO:0000313|Proteomes:UP000005275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=984 {ECO:0000313|EMBL:AHF04395.1,
RC ECO:0000313|Proteomes:UP000005275};
RG DOE Joint Genome Institute;
RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007031; AHF04395.1; -; Genomic_DNA.
DR RefSeq; WP_005223643.1; NZ_CP007031.1.
DR AlphaFoldDB; W0E0J0; -.
DR STRING; 765910.MARPU_11480; -.
DR KEGG; mpur:MARPU_11480; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_2_6; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000005275; Chromosome.
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:AHF04395.1};
KW Pyruvate {ECO:0000313|EMBL:AHF04395.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005275}.
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 529..604
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 605 AA; 65543 MW; AD98F3F4263FAE6D CRC64;
MPKINITDVI LRDAHQSLIA TRMRTEDMLP ICPKLDAIGF WSLECWGGAT FDACVRFLKE
DPWERLSRLR EALPNTRLQM LLRGQNLLGY RHYSDDVVRA FVTRAAANGM DVFRIFDALN
DLRNLKTAIE ATKAAGKHAQ GTICYTVSPA HDTAGFVRMG RELAEMGCDS IAIKDMAGLL
TPFATAELVK ALKDSVELPL HLHSHATSGL ADMCHLKAIE NGCDTIDTAI SAFAGGTSHP
PTESLVAALR GTEYDTGLDL EAIQEVGIYF HQVRKKYHQF ESDFTGVDTR VQVNQVPGGM
ISNLANQLRE QNALDRMEAV LAEIPKVRKD LGYPPLVTPT SQIVGTQAVL NVLTEKRYES
ITNEVKGYLQ GRYGQAPAPV DAALQRQAIG NAEAIDCRPA DLLEPELARL QGEIGALAEG
DEDVLTYAMF PEIGRAFLEQ RAAGTLQPEP LEPPPSETAA NAPTEFNVAV HGETYHIKVT
GAGHKGQADR HFYFTIDGVP EEVVVETLDE LVLTGGAEGA VAQKIAGKRP RPSAPGHVTT
SMPGNIVDVL VAEGDRVEAG QPLLITEAMK METEIQAPIA GTVTEVFVAK GDSVSPDEVL
IAIEA
//
