ID A0A224WXX1_9LACT Unreviewed; 1137 AA.
AC A0A224WXX1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=RsY01_567 {ECO:0000313|EMBL:GAX46987.1};
OS Lactococcus reticulitermitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2025039 {ECO:0000313|EMBL:GAX46987.1, ECO:0000313|Proteomes:UP000218689};
RN [1] {ECO:0000313|Proteomes:UP000218689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs-Y01 {ECO:0000313|Proteomes:UP000218689};
RA Ohkuma M., Yuki M.;
RT "Draft genome sequence of Lactococcus sp. strain Rs-Y01, isolated from the
RT gut of the lower termite Reticulitermes speratus.";
RL Submitted (AUG-2017) 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:GAX46987.1}.
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DR EMBL; BEDT01000001; GAX46987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A224WXX1; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000218689; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
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:GAX46987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218689}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 525..793
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1062..1137
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 199
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 703
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 732
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 734
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 867
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 703
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1103
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1137 AA; 126189 MW; 9768E29F12554866 CRC64;
MKKLLVANRG EIAIRVFRAC NELGISTVAI YAKEDEYSVH RFKADEAYQV GAGKKPIDAY
LDSDDIVRIA LESGAEAIHP GYGLLSENID FARKVEAAGL IFVGPTLHHL DIFGDKIKAK
EASIAAGVGS IPGTEGPVDL EGALAFGRTF GYPVMIKAAL GGGGRGMRVA HNEAEARDGY
ARAASEAKSA FGSDEIYVEK YITNPKHIEV QILGDAHGNV VHLYERDCSV QRRNQKVIEV
APSVGMSDDL RQRICDAAVK LCQHVGYVNA GTVEFLVKDN EFYFIEVNPR VQVEHTITEV
VTGIDIVQAQ ILIAEGADLH KDVKIPEQDK MPLLGSAIQC RITTEDPENN FLPDTGKIDT
YRSPGGFGVR LDVGNAYSGY EVTPYFDSLL VKVITNATDF KEAIRKMDRC LREFRIRGVK
TNIPFLRNVL NHSEFVSGEA KTTFIDSTPE LFSFPRLRDR GNKTMKYIAN ITVNGFPGVN
QTAKPYFDET RYPKVKKIET LTTKNILETK GADAVVDYVK SRKEVLLTDT TFRDAHQSLL
ATRVRLQDMR QVAAAVDQGL PNLFSSEMWG GATFDVAYRF LNESPWYRLR ELRKLMPNTM
FQMLFRGSNA VGYQNYPDNV IQEFIKVAAE EGIDVFRVFD SLNWLPQMEK SIQAVRDTGK
IVEATMCYTG DILDDNRQKY NIKYYKDLAK ELQATGAHIL AIKDMAGILK PQAAYRLISE
LKETVDMPLH LHTHDTSGNG IITCSAAVTA GVDIVDVATA AMSSGTSQPS MSSLYYALEN
GKRAPELDIE NAAQINHYWE DVRKFYAPFE KGLTSPQTEV YLHEMPGGQY TNLQSQATAV
GLGLRFDEVK AMYHTVNMMF GDIIKVTPSS KVVGDMALFM VQNDLTEADI YEKGASLSFP
ESVISFFAGD LGQPVGGFPE KLQKIILKDK PFITDRPGLH ATPVNFDDVV VELTEKLGYA
PGRHEVLSYI LYPQVFLDYQ KMQNEFGSVT LLDTPTFFNG MRVGEKISVQ IEKGKTLLIR
LDSISEPDNE GNKTLFFNLN GQRREMVVKD TSIKTTAVVK EKAEPSNPNH IGATMPGSVV
TVLVKPDEKV VKGQPLMVTE AMKMETTIEA PFDGEVKRIY VKAAEAIATQ DLLIEMK
//
