ID A0A1H9L6C0_9BACI Unreviewed; 1147 AA.
AC A0A1H9L6C0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216362_14413 {ECO:0000313|EMBL:SER06779.1};
OS Piscibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX NCBI_TaxID=571933 {ECO:0000313|EMBL:SER06779.1, ECO:0000313|Proteomes:UP000199427};
RN [1] {ECO:0000313|EMBL:SER06779.1, ECO:0000313|Proteomes:UP000199427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21633 {ECO:0000313|EMBL:SER06779.1,
RC ECO:0000313|Proteomes:UP000199427};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOES01000044; SER06779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9L6C0; -.
DR STRING; 571933.SAMN05216362_14413; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000199427; 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:SER06779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199427}.
FT DOMAIN 6..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 535..803
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1072..1147
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 713
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
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 744
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 877
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 713
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1113
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1147 AA; 129200 MW; 3C5410AB8E9C8BAB CRC64;
MNEVKPFNKV LVANRGEIAI RVFRACTELN IRTVAIYSEE DTGSYHRYKA DEAYLVGVGK
KPIDAYLDIE GIISIAKRVG VDAIHPGYGF LSENVHFAKR CEEEGITFIG PSSHLLDIFG
DKVKARHQAI KADIPVIPGS DGPVSSLEEV EEFVSNYGFP IMIKAALGGG GRGMRIVRTK
DSLKEAYERA KSEARAAFGS DEVYVEKLIE NPKHIEVQIL GDHQGHIVHL YERDCSVQRR
HQKVVEVAPS VSLDDQQREQ ICQAAVKLMN SVDYVNAGTV EFLVTDDEFY FIEVNPRVQV
EHTITEMITG VDIVQTQIHI AMGYELHESP IDIPKQNQIS THGFAIQSRV TTEDPLNNFM
PDTGKIMAYR TGGGFGVRLD AGNGFQGAVI SPHYDSLLVK VSTWALTFEQ AAKKMVRNLK
EFRIRGIKTN IPFLENVILH EKFLNGTYDT TFIDRSPELF VFPKRRDRGT KLLTYLGHTT
VNGPGNQGQV KKPLFSKPRI PKVDLNQDYP KGTKQLLDEK GPEAVAEWLK NTREVQLTDT
TFRDAHQSLL ATRVRTKDLL DIAEPTAKLL PNLFSVEMWG GATFDVSYRF LRENPWERLS
KLREKMPNVL FQMLLRASNA VGYKNYPDNV IENFVEKSAQ MGIDVFRIFD SLNWVEGMKP
AIEAVRKQGK IAEASMCYTG DILDPNRPKY DLEYYLKLAK ELEEAGAHIL GIKDMAGLLK
PEAAYRLIKA LKEEISIPIH LHTHDTSGNG IMMYSKAVEA GVDAVDVAVS SMAGSTSQPS
ANSLYYALEH DKRQPKLDIH AYDELARYWE DVREYYAPYE NGLKAPHSEI YFHEMPGGQY
SNLQQQAKAV GLGERWDEVK SMYRKVNDMF GDIIKVTPSS KIVGDMALFM VQNDLTVDDV
YEQGESLDFP DSVVEFFQGY IGQPYQGFPK ELQRIVLKGR EAIDSRPGEH LKPVNFEALK
EQLYEKLDRQ VTDLEIISYA LYPKVFDEYQ DFVETYGDVS VLDTPAFLYG LRLGEETAVE
IEQGKTLIVK LVSIGEAQKD GNRVVYFELN GQPREVVVRD ENVENVLQQR VKADKNNPNH
IGASMPGTVI NVLVNEGEKV SKNDHLMITE SMKMETTIQA PFEGVVKSIY VKNGEAIESG
DLLIEIE
//
