ID Q1YG44_AURMS Unreviewed; 1154 AA.
AC Q1YG44;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=SI859A1_02984 {ECO:0000313|EMBL:EAS49381.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS49381.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS49381.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS49381.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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 -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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:EAS49381.1}.
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DR EMBL; AAPJ01000005; EAS49381.1; -; Genomic_DNA.
DR RefSeq; WP_009210801.1; NZ_CH672387.1.
DR AlphaFoldDB; Q1YG44; -.
DR HOGENOM; CLU_000395_0_1_5; -.
DR OrthoDB; 9763189at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_02984-MONOMER; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000321; 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:UniProtKB-UniPathway.
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; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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:EAS49381.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT DOMAIN 2..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 539..807
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1077..1152
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 620
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 717
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 746
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 748
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 881
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 717
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1118
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1154 AA; 126391 MW; 189E90EC41B5275F CRC64;
MAIRKILVAN RSEIAIRVFR AANELDIRTV AIWAEEDKLA LHRFKADESY QVGRGPHLSK
DMGPIESYLA IEEVIRVAKL SGADAIHPGY GLLSESPEFV DACVEAGITF IGPSADTMRR
LGNKVAARNL ALEVGVPVVP ATVPLPDDMD EVRRMAAEVG YPVMLKASWG GGGRGMRAIR
DEKDLEREVV EGKREARAAF GKDEVYLEKL IERARHVEVQ ILGDTHGNVV DLFERDCSIQ
RRNQKVVERA PAPYLDDAQR AEIAGYARKL ADATAYVGAG TVEFLMDADS GKFYFIEVNP
RIQVEHTVTE EVTGIDIVKA QIHILDGHAI GTPESGVPPQ SEIRLNGHAM QCRITTEDPE
QNFIPDYGRI TAYRGATGFG IRLDGGTAYS GAVITRFYDP LLEKVTAWAP SPEEVIARMD
RALREFRIRG VATNLTFLEA IISHPKFRDN SYTTKFIDET PALFDQVKRR DRATKLLTYL
ADVTVNGHPE TKNRPRPSAE HALPIPPLFK APIVDGTRQK LDELGPRGFA DWMLAQPQVL
VTDTTMRDGH QSLLATRVRT HDIAAVADAY ARGLPQLLSL ECWGGATFDV AMRFLTEDPW
ERLALVRERA PNILLQMLLR GSNGVGYTNY PDNVVKRFVA EAARGGVDLF RVFDCLNWVE
NMRVSMDAVC EADKLCEGAI CYTGDLFDPD RAKYDLKYYV SLAKEMEAAG AHILGVKDMA
GLLKPAAARV LFKALKEEVG LPIHFHTHDT SGISAATVLA AIDFGVDAVD AAMDAFSGNT
AQPCLGSIVE ALKGSERDSG LSAEAIRRIS FYWEAVRNQY AAFESDLKGP ASEVYLHEMP
GGQFTNLKEQ ARSLGLETRW HQVAQTYSDV NRMFGDIVKV TPSSKVVGDM ALMMVSQDLT
VADVMDPKKD LAFPDSVVSM MHGDLGQPPQ GWPADIQKKV LKGETPITVR PGSLLADADL
AAEQAKLEEK LERDASAQEF ASYLMYPKVF TDFAAAQELY GPVSMLPTPS YFYGIAQDEE
VLIDLERGKT LVVRCLGFGE TDEKGMRTVF FELNGQPRRI KVPDRAHGAA GAAVRPKAEA
GNANHVGAPM PGVVSTLAVA AGQTVRSGDV LLSIEAMKME TAIHAERDGT IEAVHVTAGA
QIDAKDLLVV YAAG
//
