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Database: UniProt
Entry: Q2HF75_CHAGB
LinkDB: Q2HF75_CHAGB
Original site: Q2HF75_CHAGB 
ID   Q2HF75_CHAGB            Unreviewed;      1154 AA.
AC   Q2HF75;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 91.
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=CHGG_01129 {ECO:0000313|EMBL:EAQ92894.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92894.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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|PIRNR:PIRNR001594};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; CH408029; EAQ92894.1; -; Genomic_DNA.
DR   RefSeq; XP_001220350.1; XM_001220349.1.
DR   AlphaFoldDB; Q2HF75; -.
DR   SMR; Q2HF75; -.
DR   STRING; 306901.Q2HF75; -.
DR   GeneID; 4387604; -.
DR   VEuPathDB; FungiDB:CHGG_01129; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   HOGENOM; CLU_000395_1_1_1; -.
DR   InParanoid; Q2HF75; -.
DR   OMA; YAIQSRV; -.
DR   OrthoDB; 1129179at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001056; 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; 3.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
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; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 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; 3.
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; SSF51246; Rudiment single hybrid motif; 2.
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; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|PIRSR:PIRSR001594-
KW   2}; Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          1..450
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          47..247
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          536..804
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1074..1149
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          319..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         545
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         617
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         743
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         745
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         878
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         1115
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1154 AA;  126624 MW;  967F5D33CC0E3403 CRC64;
     MFDLDTLFPM PYQHMMLIRF LLHRSSEPSS DPLPYVIDSL GDKVSARKIA IAAGVPVVPG
     TEGAVEKFED VKKFTDQYGF PVIIKAAYGG GGRGMRVVRD EATLQESFER ASSEAKSAFG
     NGTVFVERFL DKPKHIEVQL LGDNYGNLVH LYERDCSVQR RHQKVVEIAP AKDLPADVRD
     NMLRDAVKLG RSVGLPRQDI ANICGIDIVA AQIQIAAGAT LEQLGLTQDR ISTRGFAIQT
     RITTHVIPVH PFIATRELTM LNSEDPAKNF QPDTGKIEVY RSAGGNGIRL DGGNGFAGAV
     ITRFGPVSVI LHNDNGVNTP AARADTPRNS VAGFDNNSTS KPSEPRSTGQ SQRTSSTLEG
     PRYLLVARQR LAMHSSENVF DNIFDNSEDN IKKKKMSSTR LRIMSSMLRA LIEFRIRGVK
     TNLPFITSLL THPVFIESKC WTTFIDSTPE LFDLVGSQNR AQKLLAYLGD VAVNGSSIKG
     QIGEPKFKGD IIIPELFDES GHKIDTTLPS TKGWRQIILE QGPKAFAKAI RNYKGCLLMD
     TTWRDAHQSL LATRVRTVDL LNIAKETSHA LHNLYSLECW GGATFDVAMR FLYEDPWDRL
     RKMRKLIPNI PFQMLLRGAN GVAYASLPDN AIDHFVDQAK KNGVDIFRVF DALNDINQLE
     VGIKAVQKAG GVCEGTVCYS GDMLNPTKKY NLAYYLDLVD KLVALDIDVL GIKDMAGVLK
     PHAATLLIGS IREKYPDLPI HVHTHDSAGT GVTSMVACAM AGADAVDAAT DSLSGMTSQP
     SINAILASLD GTGKDPGLNP QHVRALDTYW SQLRLLYSPF EAHLAGPDPE VYEHEIPGGQ
     LTNMMFQASQ LGLGSQWLET KKAYEHANDL LGDIVKVTPT SKVVGDLAQF MVSNKLSPED
     VKARAAELDF PGSVLEFFEG MMGQPYGGFP EPLRTNALRG RRKLDQRPGL FLDPIDFGNV
     KKELGRKFGG SVTECDIASY IMYPKVFEDY KNFVVKYGDL SVLPTKYFLS KPEIGEEFHV
     ELEKGKVLIL KLLAVGPLSE NTGQREVFYE MNGEVRQVSV DDKMAAVENV SRPKADPTDT
     SQVGAPMAGV LVELRVHDGT EVKKGDPLAV LSAMKMEMVI SAPHNGVVSQ LAVREGDSVD
     GSDLVCRIVK ADAK
//
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