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Database: UniProt
Entry: A0A372LSE3_9BACI
LinkDB: A0A372LSE3_9BACI
Original site: A0A372LSE3_9BACI 
ID   A0A372LSE3_9BACI        Unreviewed;      1146 AA.
AC   A0A372LSE3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:RFU71135.1};
GN   ORFNames=D0469_04135 {ECO:0000313|EMBL:RFU71135.1};
OS   Peribacillus saganii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=2303992 {ECO:0000313|EMBL:RFU71135.1, ECO:0000313|Proteomes:UP000264541};
RN   [1] {ECO:0000313|EMBL:RFU71135.1, ECO:0000313|Proteomes:UP000264541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V47-23a {ECO:0000313|EMBL:RFU71135.1,
RC   ECO:0000313|Proteomes:UP000264541};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (AUG-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   -!- 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:RFU71135.1}.
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DR   EMBL; QVTE01000008; RFU71135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372LSE3; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000264541; 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: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:RFU71135.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264541}.
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          1066..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   1146 AA;  127806 MW;  0189180D73FACE2A CRC64;
     MERRITKVLA ANRGEIAIRV FRACTELNIR TVAIYSKEDS GSYHRYKADE AYLVGEGKKP
     IDAYLDIEDI IRIAKNSGVD AIHPGYGFLS ENIDFARRCE EEGIIFIGPG TKHLDMFGDK
     VKARVQAELA SIPVIPGSNG PVKSLEDIIQ FGKAEGFPII IKASLGGGGR GMRIVNKLEE
     VRESYDRAKS EAKAAFGNDE VYVEKLIQNP KHIEVQILGD RHGNIVHLYE RDCSVQRRHQ
     KVVEVAPSVS IPNELRQEIC DAAVSLMKNV DYVNAGTVEF LVANGEFYFI EVNPRVQVEH
     TITEMITGVD IVQSQILIAE GHEIHGDVLG IPAQEEIKTH GFAIQSRITT EDPLNNFMPD
     TGKIMAYRSS GGFGVRLDAG NAFQGAIITP YYDSLLVKLS THALTFEQAS AKMIRNLKEF
     RVRGIKTNIP FLENVVKHEK FKTGQYDTSF IDTTPELFAF PIRKDRGTKM LSYIGNVTVN
     GFPGIEKKKK PMIEKPAIPA LGSDFRLQTG TKQILDEKGA DGLVNWVKEQ KKVLLTDTTF
     RDAHQSLLAT RIRTTDIMQI AEPAAKLLPD LFSFEMWGGA TFDVAYRFLK EDPWDRLLGL
     REKIPNVMFQ MLLRASNAVG YKNYPDNVIR EFVEKSAIAG IDVFRIFDSL NWVKGMEVAI
     DAVRQSGKIA EAAICYTGDI NDPSRTKYDI NYYKNLAKEL ENQGAHILGI KDMAGLLKPQ
     AAYRLISELK ETISIPIHLH THDTSGNGIY MYAKAIEAGV DIVDTALGAM AGLTSQPSSE
     TLYYALEGTG RQPDADVRSL QQLSHYWEIV RKYYQDFESG MISPHSEVYE HEMPGGQYSN
     LQQQAKAVGL GSRWEEVKEM YQRVNAMFGD IVKVTPSSKV VGDMALFMVQ NEMTEEDVLA
     KGEKVDFPDS VIELFEGYLG QPHGGFPQEL QRVILKGKAP LTVRPGELLD DVDFSSLKEE
     LFKEIGRPVT SFDTLAYALY PKVFLEYIKT REQFGDVSNL DTLTFLYGME LGEEIEVEIE
     KGKTLIVKLV SLGQPHADGT RVVYFELNGQ PREVIIRDES VKSAVVTKVK ADLKKESHIG
     ATMPGTVIKV LVEKGDIVSR GDHLIITEAM KMETTVQAPF SGEIKEIYVS NGEAISTGDL
     LIEISK
//
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