ID A0A099F258_9RHOB Unreviewed; 1144 AA.
AC A0A099F258;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN ORFNames=IT41_08940 {ECO:0000313|EMBL:KGJ04780.1}, SAMN04487972_10871
GN {ECO:0000313|EMBL:SFA51156.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04780.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ04780.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04780.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ04780.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04780.1,
RC ECO:0000313|Proteomes:UP000029846};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFA51156.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA51156.1,
RC ECO:0000313|Proteomes:UP000182312};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000256|PIRNR:PIRNR001594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953,
CC ECO:0000256|PIRNR:PIRNR001594};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; JRKN01000009; KGJ04780.1; -; Genomic_DNA.
DR EMBL; FOJO01000008; SFA51156.1; -; Genomic_DNA.
DR RefSeq; WP_036740312.1; NZ_JRKN01000009.1.
DR AlphaFoldDB; A0A099F258; -.
DR STRING; 376733.SAMN04487972_10871; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006090; P:pyruvate metabolic process; 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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01235; pyruv_carbox; 1.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:KGJ04780.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029846}.
FT DOMAIN 1..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 531..799
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1062..1144
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 482..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 540
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 709
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 740
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 873
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 709
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1110
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1144 AA; 125114 MW; BE9C98E1B38AC13E CRC64;
MFRKILIANR GEIAIRVMRA ANELGKKTVA IYAEEDKLGL HRFKADEAYR IGAGLGPVAA
YLSIPEIIRV ARESGADAIH PGYGLLSENP EFVDACVKAG ITFIGPRAET MRALGDKASA
RKVAIGAGVP VIPATEVLGD DFDAIKAEAA AIGYPLMLKA SWGGGGRGMR PITGPDELVE
KVREGRREAE AAFGNGEGYL EKMIQRARHV EVQLLGDTHG GLYHLYERDC TVQRRNQKVV
ERAPAPYLTP EQREEVCELA LKIGRAVGYQ NAGTVEFLMD MDSGNFYFIE VNPRVQVEHT
VTEEVTGIDI VQSQIMIAEG ATLADATGIK RQEDVHLQGH ALQCRVTTED PLNNFIPDYG
RLTAYRSATG NGIRLDGGTA YAGGVITRYY DSLLVKVTAH AQTPEQAIRR MDRALREFRV
RGVATNIEFV INLLKHPTFL NDTYTTKFID TTPDLFAFRK RRDRATKLLI YLADITVNGH
PETVGRPMPP AEARNPVAPR PKADPAPGTK QLLEEKGAKA VADWMLAQKR LLITDTSMRD
GHQSLLATRM RSIDMIRVAP SYAANLPGLF SVECWGGATF DVAYRFLQEC PWQRLRDIRK
AIPNLMTQML LRGSNGVGYT NYPDNVVQGF VRQAAATGID LFRVFDSLNW VENMRVAMDA
VIESGKICEG TICYTGDILD PERSKYDLKY YLNMARELRD AGAHVLGLKD MAGLLKPASA
GVLVKALKEE VGLPVHFHTH DTGGIAGASI LAAAAAGVDA VDCAMDALSG NTSQPTLGSI
VEALRHSDRD TGLDIAAIRA ISNYWEAVRE HYAAFESGLQ APASEVYLHE MPGGQFTNLK
AQARSLGLEE RWHEVAQAYA DVNRMFGDIV KVTPSSKVVG DMALMMVAQG LTPAQVIDPD
TDVSFPDSVV DMMRGNLGQP PGGWPEGLQK KVLKGEEPMT TRPGASMPPV DLEATRADLS
EQLEGKAVDD EDLNGYLMYP KVFLDYMGRH RQYGPVRTLP TRSFFYGMEP GEEIEAEIDP
GKTLEIRLQT VGETDDQGDV KVFFELNGQP RVIRVPNRLV KSQTVARPKA DPANDAHVGA
PMPGVVASVA VTQGQRVNHG DMLVTIEAMK METGIHADRA GVISALHVRP GEQIDAKDLL
VEIT
//