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Database: UniProt
Entry: G1X7J2_ARTOA
LinkDB: G1X7J2_ARTOA
Original site: G1X7J2_ARTOA 
ID   G1X7J2_ARTOA            Unreviewed;      1198 AA.
AC   G1X7J2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
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=AOL_s00054g909 {ECO:0000313|EMBL:EGX50823.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX50823.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX50823.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX50823.1}.
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DR   EMBL; ADOT01000093; EGX50823.1; -; Genomic_DNA.
DR   RefSeq; XP_011120527.1; XM_011122225.1.
DR   AlphaFoldDB; G1X7J2; -.
DR   STRING; 756982.G1X7J2; -.
DR   GeneID; 22891503; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   HOGENOM; CLU_000395_0_1_1; -.
DR   InParanoid; G1X7J2; -.
DR   OMA; YAIQSRV; -.
DR   OrthoDB; 1129179at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008784; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT   DOMAIN          36..488
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          158..355
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          574..842
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1111..1186
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         583
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         655
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         751
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         781
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         783
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         916
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         751
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1152
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1198 AA;  131978 MW;  3A20A009FEED99B7 CRC64;
     MSNQQYANVF DEEEMDGASS TARSVHRIRS NSTIMQLKKI MVANRGEIPI RIFRTAHELS
     LQTVAIYSYE DRMGMHRQKA DEAYMIGHRG QYTPVGAYLA IDEIIKIALE HNVNMIHPGY
     GFLSENAEFA RKVEEAGIIF VGPTYKVIEA LGDKVSARRI AQACKVPCVP GTPGPVEKFS
     DCDHFVKEYG YPIIIKAAFG GGGRGMRVVR EGDNLEDAFE RAVSEAKSAF GNGTVFIERF
     LDKPKHIEVQ LLGDNHGNIV HLYERDCSVQ RRHQKVVEIA PAKDLPQETR QAILDDAVRI
     AKHVNYRNAG TAEFLVDNQN RHYFIEINPR IQVEHTITEE ITGIDIVAAQ IQIAAGASLA
     QLGLTQDRIS TRGFAIQCRV TTEDPSENFR PDTGKIEVYR SAGGNGVRLD GGNGFAGSII
     TPHYDSMLVK CTCHGSTYEI ARRKVIRALV EFRIRGVKTN IPFLLSLLTH EVFINGTCWT
     TFIDDTPELF SLMKSQNRAQ KLLAYLGDLS VNGSSIKGQV GEPKFKGQII MPILTDRTGK
     VIDTTQPCQK GWRNILLEQG PEAFAKAVRA NKGCLIMDTT WRDAHQSLLA TRVRTIDICE
     IAKQTSYAYA NAYSIECWGG ATFDVAMRFL YEDPWDRLRK MRRLVPNVPF QMLLRGANGV
     AYSSLPDNAI EHFCDQARKN GVDIFRVFDA LNDVAQLEVG IKAVKKAGGV VEAAICYSGD
     MLNPKKKYNL EYYLDLADKV VKLGTHILGI KDMAGCLRPR AATILIGALR ERYPDLPIHV
     HTHDSAGTGV ASMAACAAAG ADAVDTATDS MSGMTSQPSV GAVLAALEGT DMDPGLDIEL
     VREIDSYWAQ LRLMYSCFEA GLTGPDPEVY VHEIPGGQLT NLIFQASQLG LGAQWKETKK
     AYTQANYLLG DIVKVTPTSK VVGDLAQFMV SNKLSPEDVV ERAETLDFPG SVLDFLEGLM
     GQPFGGFPEP LRTRALRGRR ALSERPGLTL HPTDLPGIKQ ELLEKYGQVT ECDVASYVMY
     PKVFLDYKEF LAKYGDLSVL PTKYFLSTPE IGEEFHVQIE KGKTLIIKLL AVGPLSEQTG
     QREVFFELNG EVRQVTVDDK KAAVENTSRL KANQADSSQV GAPMSGVVVE VRVKDGSEVK
     KGDPIAVLSA MKMEMVISAP HSGVIAELQI KANDSVDGQD LICKIVKAAT ESAEEKSD
//
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