ID A0A066XEY6_COLSU Unreviewed; 1175 AA.
AC A0A066XEY6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=CSUB01_09993 {ECO:0000313|EMBL:KDN64321.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64321.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second. {ECO:0000256|ARBA:ARBA00002380}.
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|ARBA:ARBA00000564,
CC 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:KDN64321.1}.
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DR EMBL; JMSE01001142; KDN64321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XEY6; -.
DR STRING; 1173701.A0A066XEY6; -.
DR eggNOG; KOG0369; Eukaryota.
DR HOGENOM; CLU_000395_0_1_1; -.
DR OMA; YAIQSRV; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000027238; 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 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:KDN64321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 38..486
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 156..353
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..828
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1098..1173
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 581
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 653
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 737
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 767
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 769
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 902
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 737
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1139
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1175 AA; 129159 MW; A3376ABFD3A4C556 CRC64;
MAQTAVTYND VFEEGDVEEV QKDPQTIHHI RANSSIMHLK KILVANRGEI PIRAHELSLH
TIAVFSYEDR LSMHRQKADE AYVIGKRGQY TPVGAYLAGD EIIKIAVEHG AQMVHPGYGF
LSENAEFARN VEKAGLIFVG PSADVIDSLG DKVSARKLAI AAGVPVVPGT EGAVATFEEV
KSFTDQYGFP IIIKAAYGGG GRGMRVVREQ ETLKEAFDRA TSEAKSAFGN GTVFVERFLD
KPKHIEVQLL GDNHGNIVHL YERDCSVQRR HQKVVEIAPA KDLPSEVRDA ILNDAVKLAK
SVNYRNAGTA EFLVDQQNRY YFIEINPRIQ VEHTITEEIT GIDIVAAQIQ IAAGATLQQL
GLTQDRISTR GFAIQCRITT EDPAKDFQPD TGKIEVYRSA GGNGVRLDGG NGFAGAVITP
FYDSMLVKCS CHGSTYEIAR RKVLRALVEF RIRGVKTNIP FLASLLTHPT FIDGNCWTTF
IDDTPQLFDL IGSQNRAQKL LAYLGDVAVN GSSIKGQIGE PKFKGDIILP ELLNEDGSKI
DVSQTCTKGW RQIILEQGPK AFAKAVRDYK GTLLMDTTWR DAHQSLLATR VRTVDLLNIA
KETSHGLHNL YSLECWGGAT FDVAYRFLYE DPWDRLRRMR KAVPNIPFQM LLRGANGVAY
SSLPDNAIDH FVEQAKKNGV DIFRVFDALN DIDQLEVGIK AVHKAGVLNP KKKYNLQYYL
DLVDKLVALD IHVLGIKDMA GVLKPHAAEI LIGSIRKKYP DLPIHVHTHD SAGTGVASMV
ACAKAGADAV DAATDSLSGM TSQPSINAII ASLEGSDHDT GLNPAHVRAL DSYWSQLRLL
YSPFEAHLAG PDPEVYEHEI PGGQLTNMMF QASQLGLGTQ WAETKKAYEH ANELLGDIVK
VTPTSKVVGD LAQFMVSNKL SADDVRARAG ELDFPGSVLE FLEGLMGQPY GGFPEPLRTN
ALRGRRKLDK RPGLFLEPVD FAKIKRDLHK KFGGPVTECD IAAYVMYPKV FEDYKKFIQK
YGDLSVLPTK YFLSRPEIGE EFHVELEKGK VLILKLLAIG PLSENTGQRE VFYEMNGEVR
QVTVDDNKAS VENVSRAKAD PSDSSQVGAP MAGVLVELRV KDGSDVKKGD PIAVLSAMKM
EMVISAPHNG KVSTLQVKEG DSVDGSDLVC RIVKA
//
