ID Q1L5E6_BACMT Unreviewed; 1147 AA.
AC Q1L5E6;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 13-SEP-2023, entry version 69.
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 Name=pyc {ECO:0000313|EMBL:AAY89102.1};
OS Bacillus methanolicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1471 {ECO:0000313|EMBL:AAY89102.1};
RN [1] {ECO:0000313|EMBL:AAY89102.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MGA3 {ECO:0000313|EMBL:AAY89102.1};
RA Holen H., Aakvik T., Ellingsen T.E., Brautaset T.;
RT "Sequence and transcriptional analysis of the pyruvate carboxylase gene,
RT pyc, in methylotrophic Bacillus methanolicus strains.";
RL Submitted (MAY-2005) 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};
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DR EMBL; DQ025534; AAY89102.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1L5E6; -.
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 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; 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; 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|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:AAY89102.1}.
FT DOMAIN 4..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 533..801
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1067..1145
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 542
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 711
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
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 742
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 875
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 711
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1111
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1147 AA; 128356 MW; 96427F04091AD998 CRC64;
MKRSINKVLV ANRGEIAIRV FRACTELNIR TVAIYSKEDS GSYHRYKADE AYLVGEGKKP
IDAYLDIEGI IEIAKSSGAD AIHPGYGFLS ENIEFAKRCA EEGIIFIGPE AKHLDMFGDK
VKARTQAQLA EIPVIPGSDG PVKGLEEVIQ FGKTYGFPII IKAALGGGGR GMRIVRSLEE
VREAYERAKS EAKAAFGSDQ VYVEKFIEKP KHIEVQIIGD EHGNIVHLYE RDCSVQRRHQ
KVVEVAPCVS ISSELRERIC EAAVRLMKNV NYVNAGTVEF LLSGDEFYFI EVNPRIQVEH
TITEMVTGVD IVQTQILVAE GHELHGEKIG IPKQKDIHIN GYAIQARVTT EDPLNNFMPD
TGKIMAYRSG GGFGVRLDAG NGFQGAVITP YYDSLLVKLS THAMTFEKAA AKMVRNLREF
RIRGIKTNIP FLENVVKHEK FRTGQYDTSF IDTTPELFLF PKSKDRGTKM LTYIGNVTVN
GFPGIEKRKK PVFDKPRIPK LKYDTEFKNG TKQILDELGA DGLVKWVKEQ KEVLLTDTTF
RDAHQSLLAT RIRTTDISHI AEPTAKLLPE LFSFEMWGGA TFDVAYRFLK EDPWERLLKL
RKQIPNVLLQ MLLRASNAVG YKNYPDNVIR EFVEKSAQAG IDVFRIFDSL NWVKGMEVAI
DAVRQTGKIA EAAICYTGDI SDPTRTKYDL NYYKELAVEL EKQGAHILGI KDMAGLLKPQ
AAYRLISELK ETVSIPIHLH THDTSGNGIY MYAKAIEAGV DIVDVALSSM AGLTSQPSAN
TLYYALEGTE RKPNVNIEAL EQLSHYWEDV RKYYHDFESG MMSPHTEVYQ HEMPGGQYSN
LQQQAKAVGL GDKWDQVKEM YARVNQMFGD IVKVTPSSKV VGDMALFMVQ NELTEEDILN
RGESLDFPDS VVEFFEGYLG QPHGGFPKDL QKVILKGKEP ITVRPGELLE DVDFEALKEE
LYKEIGRPVT SFDVIAYALY PKVFLEYIQT VEKFGDVSVL DTPTFLYGMR LGEEIEVEIE
TGKTLIVKLV SIGQAQADGT RVVYFELNGQ PREVIIKDES IKSAIASRVK ADPKNESHIG
ATMPGTVIKV VVKKGEKVER GDHLVITEAM KMETTVQAPF SGIVKDIFVN NGDAIQTGDL
LIELAKS
//
