ID A0A8K0JQA3_9TREE Unreviewed; 1256 AA.
AC A0A8K0JQA3;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FFLO_01868 {ECO:0000313|EMBL:KAG7562708.1};
OS Filobasidium floriforme.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Filobasidiales; Filobasidiaceae; Filobasidium.
OX NCBI_TaxID=5210 {ECO:0000313|EMBL:KAG7562708.1, ECO:0000313|Proteomes:UP000812966};
RN [1] {ECO:0000313|EMBL:KAG7562708.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 6242 {ECO:0000313|EMBL:KAG7562708.1};
RA Nowrousian M.;
RT "Analysis of mating type loci in Filobasidium floriforme.";
RL Submitted (APR-2020) 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:KAG7562708.1}.
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DR EMBL; JABELV010000027; KAG7562708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8K0JQA3; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000812966; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
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; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF128; UREA AMIDOLYASE; 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; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000812966}.
FT DOMAIN 18..475
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 136..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1172..1251
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1256 AA; 138794 MW; 6D09DBACC2F1431D CRC64;
MSTSQPRPEI VLSDGFTHIR KVLIGNRGEI ACRIIKTCKS LGLSSVSIYS PADRSSLHVR
QADEAYLLPG PDQTAYIDEQ AILDIATKSG VQAVIPGYGF LSENAGFAER VERAGLVWVG
PSSTVIKQFG LKHTARRLAM EAGVPVLTGS GLVETVEDAL KAAEDVGYPV MLKATAGGGG
MGLQICHTPS QIPSSFQTVY DRSKTLFHDP GMFVEKYIPE SRHVEVQVFG NGMGGAVHFG
ERECSIQRRH QKVVEECPSP FVHTRPGLRK RLTDCAVSLA KSVSYGSAGT VEFLVDDQTG
DFYFLEMNTR LQVEHGITEM CYDVDLVALM LQQAEMQARD QGGGIDLESL RSLQREAPRG
FAIEARIYAE VPSRNYEPSP GLLQHVEWYE AADVRIDTWV HSGTNISSFY DPMIAKMMVW
DEQSHDAATE KMVQALSRSL VQGCPTNIRF LSAIVDSQAF RKGETTTSFL TREAFDFQPA
TLDVISGGAY TTIQDWPARR GVSFGVPESG PMDAVSFRLA NVIVGNPQTM EGLEVTLIGP
ELLFNTPGII AVTGGVIDVY IDGEPVDMYM RHLVPAGKKL KLGYVTSGCR AYIAIKGGFP
SVPLYLGSKS TTSTLKLGGY QGRQLFPNDL LELDPACKEW AVHHEPFSLP ARIRLDQFWR
DDWVLYVMPG PHDDPEFVTE QDREILYSTR WKISHNATRS GYRLKGPRLR WARTSGGEGG
SHPANVIDEP YPYGGMNWNG DEPVLLPVDG PMAGGLATTT TIVRADLWRM GQCRPGNRIQ
FKRITWQSAR DLADRIEAFI EMVRRFVEGQ VGEEDLSGLD IELPDGWDET VLHTVEGDEA
SGTALVKFRQ AGDSHIQVTY GPMTASALMR SHVQQVINRI HDIEIPGVVC VTGTTRAYSV
QFHPHQISQT ALLQALVNIE NSLVKSHDPL PSRIFKFPVL LEDPIFKVAV ADYTATVRSS
AVYLPDNMDY IAKSNGVCDR ETASRSIVAC PQLVTALSFL AGTPFILPLD PRLVYVAQKY
NPTRMFTPEG TVGLGGPLLV IYPMESPGGY QFWGRSLAAW DAYANKPGFT KPWLLREFDQ
IQFYEVDQAE FDRCYEDFKT GRFRFEVEET TFDPAAYKVF LDSIEQETKD FVARRNAANL
VSGEEETRLL EVWHADSAER DGDDRSGDDV AVKTIDDRSV HVVAPMTSSV WKVLVEAGDK
VEQGQTLVIL EAMKMEIPIR ADETMDGSTV VKVVAKPGSL MDPGQTLVLL SSRSSE
//
