ID A0A2C5ZA15_9HYPO Unreviewed; 1045 AA.
AC A0A2C5ZA15;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=CDD80_1375 {ECO:0000313|EMBL:PHH76620.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH76620.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH76620.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH76620.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:PHH76620.1}.
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DR EMBL; NJES01000155; PHH76620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5ZA15; -.
DR STRING; 2004952.A0A2C5ZA15; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
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; IPR011764; Biotin_carboxylation_dom.
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; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 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 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; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000226431}.
FT DOMAIN 2..464
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 462..730
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1024..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 113684 MW; 3C5C1E9D1469FF28 CRC64;
MKQVRLLVAN RGEIASRILA AARELDMYTI AIFSAEDRFA GYRQKADESY LVGGPGIGPL
EAYLDGARIV EIAKQHQVDL VHPGYGFLAE NAGFASQVRQ AGMTFVGPPT DILEKMGDKV
AARRIAHEFK IPTIPGTDGP LSTLNEAYEF AEKHGFPIVV KASFGGGGRG IKVVHEKQSL
EAAIVSARSE AGAAFGNSAV FIERYISRPR HIEVQILSDG HGGHLHMFER DCSVQRKHQK
IVEMAPAANL PPHVRRGVLE AAVGLARGLE YENAGTVEFL VEGDRFYFIE MNPRIQVEHT
VTEEITGIDI VASQLRIACG ATLAELGLVQ EAIKIRGFAI QSRITTEIPS QGFRPDSGPI
SACNCWTTFI DDTPDLLPAQ AQTDQGLGLM RFLADGAVNG SRIKGQTGPP ALKREIDIPA
LFDLESGEPI DTTKPCLQGW RNILLRDGPR EFARQVRAHG PTLITDTTWR DGQQSLLATR
VRTRDLKAIA KHTSHAYREA YSLECWGGAT FDVALRFLWE CPWERLRQLR RLVPNVPFQM
LLRSTNGVAY SALPDNALFH FVKHAKDTGI DIFRVFDSLN DPQNLKIGIQ AVLAAGGLVE
GAVLYTSDML KPGTKYSLAY YMGVIDRLVE YGSHVIAIKS MSGVMKPAAG RALVRAIREK
YPSYPIHMHT HDTNGTGTAT MLACVEEGAD IVDTAIDSLS GSTSQPAAGA VIAGLQNTGF
ESALSLDQIS TIDAYWSQLR LLYAGFDAGG RPADPTVYKH EIPGGQYSNL LYQARENGLG
KQWDETLKAY EDANMLLGDI IKATPTSKAV GDLAQFIVDQ KLTAEQVQER ASTLDFPKSV
VEFLTGLMGQ PFDGFPEPFQ VYMDFRKVQM EFGNLTTLPT YHFLLPPDIG DEVRLEGDGG
KEVVAEMVAM RPTDPKSGNR QILFRLNGEF CFVVVPDDKA SPKQQLPKAN PDVQGEVAAP
MAGRVVRVAA NEGTVVKAGQ NLLTEVDVTS PAAGSVQAIF AQVGDTVEKG DLLVRIKGSA
ANGQKMNGSA LNGDAGNHTM RDNSF
//
