ID A0A072PP35_9EURO Unreviewed; 665 AA.
AC A0A072PP35;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Pyruvate carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_05172 {ECO:0000313|EMBL:KEF57255.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF57255.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF57255.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF57255.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF57255.1}.
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DR EMBL; AMGV01000004; KEF57255.1; -; Genomic_DNA.
DR RefSeq; XP_013259845.1; XM_013404391.1.
DR AlphaFoldDB; A0A072PP35; -.
DR STRING; 1182545.A0A072PP35; -.
DR GeneID; 25280098; -.
DR VEuPathDB; FungiDB:A1O9_05172; -.
DR HOGENOM; CLU_000395_3_2_1; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 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 SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 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:UP000027920}.
FT DOMAIN 7..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 570..651
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 665 AA; 73044 MW; 2EA246F9CF34D84D CRC64;
MPPIQRPISR ILIVNRGEIA IRILQSCQEL PNPLTTVAVY TENDNTHISL GRPDQAIKLP
SPSSYMDIDY LVGLVKEHKI DAVHPGYGFL SESAEFSHRM WTEANCLVVG PGWEVLERTG
DKLKAKALAM ECEVPVLKAM NKPTGNVHDV RTFAGQVSYP LMIKAVDGGG GRGIRLVKSQ
DSLDNAVQRC ISESPSKTVF AEQAAVDGYK HIEVQILGNG KGGVRHLWER DCSVQRRFQK
IVEVAPAPVR RRNVIAKVID SAIRMARQLK YLGLGTWEYL VNVKTRKFFF LEINPRLQVE
HTITESITGV DIVKEQLLFA QGLQDSEDLR LGEWWEADKA PPSFSIQLRL CAEDPASNFA
LSIGKVSDVH FPSGNGIRVD SHLSKGGVVG TDFDNMMAKI IVTASTFEGA VAKAKRALSE
TKIVGVKTNL NLLRAIVRGK AFALGEAATT WLENDIEKLV SDGELIGQTI EQVDSTLPAL
SLDNNQSSTI ASSGTTFRKG DAWTVTLEAK DSQSETKPPP SHFSIERIMR NEFPEALIAD
VSYTASGTQP QSYKMTIAST TSSADATAST HRRGDPNDKS HVVLPISGKL VEILVDEGDE
IQENQVIAFV KQMKMELEIR SPRAGTIKWA IELDSEDGDD VAEGVLLAEL EEQTTGKKPE
VRSRL
//
