ID A0A074U897_9RHOB Unreviewed; 1143 AA.
AC A0A074U897;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-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=DL1_13885 {ECO:0000313|EMBL:KEP70897.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP70897.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP70897.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP70897.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEP70897.1}.
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DR EMBL; JHEH01000004; KEP70897.1; -; Genomic_DNA.
DR RefSeq; WP_038063413.1; NZ_JHEH01000004.1.
DR AlphaFoldDB; A0A074U897; -.
DR STRING; 1185766.SAMN05216224_102568; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000027725; 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 Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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:KEP70897.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027725}.
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 1068..1143
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 480..509
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 1109
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1143 AA; 124772 MW; A10BFD76BDF1608D CRC64;
MFNKILVANR GEIAIRVMRA ANELGKKTVA VYAEEDKLGL HRFKADEAYR IGEGLSPVGA
YLSIEEIIRV ALASGADAIH PGYGLLSENP DFVDACVNAG ITFIGPKAET MRALGDKASA
RQVAIKADVP VIPATNVLGE DFDAIKREAA EIGYPLMLKA SWGGGGRGMR PITSEAELVE
KVREGRREAE AAFGNGEGYL EKMILRARHV EVQLLGDTHG GLYHLYERDC TVQRRNQKVV
ERAPAPYLSE AQREEVCALA LKIGRAVGYQ NAGTVEFLMD METDQFYFIE VNPRVQVEHT
VTEEVTGIDI VQAQIRIAEG ATLAEATGTP SQNDVTLSGH ALQCRVTTED PQNNFIPDYG
RITAYRSATG NGIRLDGGTA YAGGVITRYY DSLLVKVTAW AQDPDQAIRR MDRALREFRI
RGVSTNIDFV INLLKHPTFI DMSYSTKFID TTDALFDFKQ RRDRGTKILT YIADITVNGH
PETAGRPKPS AEARPPRVPE AIGTPQPGTR NLLEEKGPKA VAEWMKGQKK LLLTDTTMRD
GHQSLLATRM RSIDMIKAAP AYAANLGDLF SVECWGGATF DVAYRFLQEC PWQRLRDIRS
HLPNVMTQML LRASNGVGYT NYPDNVVQFF VKQAAETGVD VFRVFDSLNW VENMRVAMDA
VIESGKLCEG TICYTGDMLD PDRAKYDVKY YVGMAKELEA AGAHVLGLKD MAGLLKPAAA
RQLISALKDE IGLPIHFHTH DTSGISGATV LAAADAGVDA VDAAMDAFSG GTSQPCLGSI
VEAMAHTERD TGLDIGAIRM MSNYWEAVRH QYAAFESGLE APASEVYLHE MPGGQFTNLK
AQARSLGLEE RWHEVAQAYA DANQIFGDIV KVTPSSKVVG DMALMMVSQG LSKADVLNPA
KDMSFPDSVI DMLRGNLGQP PGGWPAEISQ KVLKDENPST ERPGKHLPAV DIEATRKTLA
EELDCEIDNE DLAGYLMYPK VFTEYATRHE TYGPVRALPT PTFFYGLEPQ TEISAEIDPG
KTLEIRYLTT GETDELGDVK VYFELNGQPR AVRVPNRAVK ATTAAKPKAD ISNPNHIGAP
MPGSIASVAV SVGQAVKAGD LLLTIEAMKM ETGLHADRDA TVKAVHVSPG TQIDAKDLLI
ELE
//
