ID A0A2S0WVS1_9MICO Unreviewed; 1134 AA.
AC A0A2S0WVS1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=DCE93_06280 {ECO:0000313|EMBL:AWB95314.1}, DCE94_09765
GN {ECO:0000313|EMBL:PWC04410.1};
OS Agromyces badenianii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=2080742 {ECO:0000313|EMBL:AWB95314.1, ECO:0000313|Proteomes:UP000244729};
RN [1] {ECO:0000313|EMBL:AWB95314.1, ECO:0000313|Proteomes:UP000244729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30A {ECO:0000313|Proteomes:UP000244729}, and MF30-A
RC {ECO:0000313|EMBL:AWB95314.1};
RA Li J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWC04410.1, ECO:0000313|Proteomes:UP000245232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=845 {ECO:0000313|EMBL:PWC04410.1,
RC ECO:0000313|Proteomes:UP000245232};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) 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; CP028913; AWB95314.1; -; Genomic_DNA.
DR EMBL; QEFA01000002; PWC04410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WVS1; -.
DR KEGG; agm:DCE93_06280; -.
DR OrthoDB; 9760256at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000244729; Chromosome.
DR Proteomes; UP000245232; 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; 1.
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; 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:AWB95314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244729}.
FT DOMAIN 1..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 529..798
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1058..1132
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 296
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 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 538
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 610
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 708
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 737
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 739
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 872
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 708
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1098
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1134 AA; 121933 MW; EADF1761AADFBAA0 CRC64;
MFTKILVANR GEIAIRAFRA AVELGAKTVA VYPYEDRNSL HRLKADEAYQ IGEPGHPVRA
YLDVTEIIRV AQLSGADAIY PGYGFLSENP ELAQAAEAAG ITFIGPPKRV LEMAGNKVTA
KEHAIAAGVP VLKSTPPSRD IETLVAQADE VGFPIFAKAV AGGGGRGMRR VSTKDELRPA
LEEAMREADS AFGDATMFLE QAVLRPRHIE VQVLADATGE TVHLFERDCS VQRRHQKVIE
IAPAPNLSDE VRQSLYRDAI AFAKSIGYVN AGTVEFLLDT AGERAGQHVF IEMNPRIQVE
HTVTEEVTDV DLVVSQIRIA AGESLTQLGL QQDSIRLRGA ALQCRITTED PTAGFRPDTG
KITTYRSPGG AGIRLDGGTI NPGAQISPHF DSMLAKLTCR GRDYPAAVAR AKRALAEFRI
RGVSTNIPFL QAVLEDPAFV AGDLSTSFID ERPQLLRGRV SKDRGTKILN WLADVTVNQP
NGPAPTTVSP AEKLPAIDIT APAPAGSRQR LLELGPLGFA QALRAQTPLA VTETTFRDAH
QSLLATRVRT RDLVAVAPYV ARMTPELLSV EAWGGATYDV ALRFLGEDPW ERLAALRGAL
PNINIQMLLR GRNTVGYTPY PTEVTDSFVR EAAATGVDIF RIFDALNDVS QMRPAIDAVL
STGHAVAEVA VCYTGDLLDP AEDLYTLDYY LALAEKIVDA GAHVLAIKDM AGLLRPTAAE
KLVTALRERF DLPVHLHTHD TAGGQLATLL AASRAGVDAV DVASAPMAGT TSQPSASSLV
AALAHTERDT GISLDAVSDL EPYWEAVRRL YRPFESGLPG PTGRVYHHEI PGGQLSNLRQ
QAIALGLADD FELIEDMYAA ADRILGRVPK VTPSSKVVGD LALHLAAVKA DPADFAANPE
KYDVPDSVIG FMAGELGDLP GGWPEPFRTK VLAGKDVRIG VTELTTEQRT ALEADSTTRR
ATLNTLLFPA PTRQFEQIRE LFGDLSVVDT ADYLYGLRQG AEHVVEIDPG VRLYAGLEAI
GEADDKGMRT VMTILNGQLR PVFVRDRSID VETRAAEKAD ASQPGQIPAP FSGVVTLQVE
VGDEIAAGQS VASIEAMKME AAITSPVAGV IERVAIPKTQ QVEAGDLLVV VRPR
//
