ID A0A8T6R5S5_9MICO Unreviewed; 1126 AA.
AC A0A8T6R5S5;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
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=EPD83_014320 {ECO:0000313|EMBL:NHA69216.1};
OS Phycicoccus flavus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Intrasporangiaceae; Phycicoccus.
OX NCBI_TaxID=2502783 {ECO:0000313|EMBL:NHA69216.1, ECO:0000313|Proteomes:UP000287866};
RN [1] {ECO:0000313|EMBL:NHA69216.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CMS6Z-2 {ECO:0000313|EMBL:NHA69216.1};
RA Tuo L.;
RT "Phycicoccus flavus sp. nov., a novel endophytic actinobacterium isolated
RT from branch of Kandelia candel.";
RL Submitted (MAR-2020) 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=hydrogencarbonate + pyruvate + ATP = oxaloacetate + ADP +
CC phosphate + H(+); 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 -!- 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:NHA69216.1}.
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DR EMBL; SAYU02000051; NHA69216.1; -; Genomic_DNA.
DR RefSeq; WP_165566748.1; NZ_SAYU02000051.1.
DR AlphaFoldDB; A0A8T6R5S5; -.
DR Proteomes; UP000287866; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR FunFam; 3.20.20.70:FF:000120; Pyruvate carboxylase; 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 InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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; CPAse_ATP-bd.
DR InterPro; IPR055268; PCB-like.
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; NF006761; PRK09282.1; 1.
DR NCBIfam; NF009554; PRK12999.1; 1.
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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:NHA69216.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287866}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 525..794
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1051..1125
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 292
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 534
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 704
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 733
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 735
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 868
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 704
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1091
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1126 AA; 121095 MW; 1B171A14EF8058AD CRC64;
MFHKILVANR GEIAVRAFRA ATELGAKTVA VFPHEDRNSE HRLKADESYE IGEEGHPVRA
YLDHEQVVAV AVACGADAVY PGYGFMSENP DLAEACEAAG ITFIGPPASA LHLAGNKARA
IAAAREAGLP TLRGAEPSTD LDVLAAAADE IGFPVFVKAV SGGGGRGMRR VDDPGTLRES
LEAAQREADA AFGDPTLYLE EAVVRPRHIE VQVLADAEGE VLHLFERDCS VQRRHQKVVE
IAPAPNLDQG LRDRICADAV RFAQAIGYRN AGTVEFLLGE DGRYVFIEMN PRIQVEHTVT
EEVTDVDLVA SQMRIAAGAT HADLGLAQDE IRTRGAALQC RITTEDPANG FRPDAGQITV
YRSAGGGGVR LDGGTVFVGA QVSPHFDSML VKLTCRGRDF DAAVRRARRA LAEFRIRGVS
TNIPFLQAVL DDPAFQRGEA TTSFIDERPE LLDARTPADR GTKLLQYLAD VTVNRPHGPA
TTHLKARTKL PPLDTGAPLP PGTRDLLLRV GPAEFARQLR ARPDVPVTDT TFRDAHQSLL
ATRMRTRDLL HVAGHVARLT PQLLSMEAWG GATYDVALRF LHEDPWERLA LLRQAMPNVP
LQMLLRGRNT VGYTPYPTKV TDAFVHEAAR TGLDVFRIFD SLNDVSQMRP AVEAVLETNT
AVAEVCLCYT GNLMDPGEDL YTLDYYLRLA EEIVDTGAHV LAVKDMAGLL RAPAARRLVT
ALRENFDLPV HLHTHDTAGG QIGTLLAAID AGVDAVDAAT ATMAGTTSQP SLSALVAATD
GTERETGLDI DAVFSLEPYW EAVRRVYAPF ESGLASPTGR VYFHEIPGGQ LSNLRQQAIA
LGLGEKFEAV EDMYAAANRI LGNLVKVTPS SKVVGDLALA LVGAGADPAD FEADPQSYDI
PDSVLGFLAG ELGDPPGGWP EPFRTKALEG RSAKPRVTEL TTEQEAALVT DTRRTLNTLL
FPGPTQEYEE TRELYGDLSV LGTIEFLHGL EHGTEYEAEI EPGKTLLLGI SSVGEVDRQG
MRTVMCTLNG QFRPVQVRDR SVEAETKAAE KADPGDRGHV AAPFAGVVTP TVQEGQDVEA
GAVVATIEAM KMEANITTPV GGTVARLAVD GHQQVEGGDL VAVIAS
//
