GenomeNet

Database: UniProt
Entry: A0A099F258_9RHOB
LinkDB: A0A099F258_9RHOB
Original site: A0A099F258_9RHOB 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system