ID A1CNQ7_ASPCL Unreviewed; 1250 AA.
AC A1CNQ7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE SubName: Full=Urea amidolyase, putative {ECO:0000313|EMBL:EAW07278.1};
GN ORFNames=ACLA_019830 {ECO:0000313|EMBL:EAW07278.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07278.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07278.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; DS027059; EAW07278.1; -; Genomic_DNA.
DR RefSeq; XP_001268704.1; XM_001268703.1.
DR AlphaFoldDB; A1CNQ7; -.
DR STRING; 344612.A1CNQ7; -.
DR EnsemblFungi; EAW07278; EAW07278; ACLA_019830.
DR GeneID; 4701460; -.
DR KEGG; act:ACLA_019830; -.
DR VEuPathDB; FungiDB:ACLA_019830; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_002162_0_1_1; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000006701; 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_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:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000006701}.
FT DOMAIN 3..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1155..1235
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1101..1135
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1250 AA; 136986 MW; C12B558F3B176DAB CRC64;
MDSLKTLLVA NRGEIAVRIV KTAKKLNIRT IAIYTEPDAS SIHVHQADEA VLLHGSPSQA
YIDGEQIIQV ATQHKVDAII PGYGFLSENA DFARAVATAG MVFVGPSPES IEAFGLKHTA
RDLATKAGAP IVPGSPGLVK SEEEAVTLAK ALGFPVMLKA TAGGGGMGLL TCSSEAEVRK
AFATVKSRGE ALFKNAGLFI ERYYPSSHHI EVQVFGNGNG KAIYIGEREC SIQRRHQKVI
EECPSPLVSR NPGLRKALGE AAVRLAESIN YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
HGITELCYGL DLVELMLKQA DAQLSGSKGI EASFLASLPI ENPSGAAIEA RVYAENPIRD
FAPSPGTLQS VEWKEIPGSR IDTWVYRGIK VSANYDPLLA KVMYHSPDRQ QTIAGLRDML
KESRICGPPT NLEFLAKILD SEEFAAGNTL TRFLDTFQFA PCAIDVISGG SYTLIEDWPG
RPALGKGFCH SGPMDPLAFR VANALVGNPI GREGLEITLS GPDLRFLGPA IVSLCGAPIE
AKLDGKPIRM WSRVKVDAGQ RLTIGRTTGN GCRTYLAVFG GFLNVAEWFG SKSTSPMVGV
GGYQGRQLSS GDLLTITSDV PDLIGDILIP EHLIPKYPSD WELLAIPGPY DEGFLTPESI
DVLFDTQWKI SHNAARGGIR LIGPKPTWAR SDGGEGGAHP SNLIEYGYAI GSLNWTGDDP
VIFPQDAPDF GGFVSSHTIV KADLWKLGQV KAGDTLKYRA VALADALDAR RDMERFVDEL
VNACKQGQGF GYVVPLQHMP PEQTAKTRGK GIVHQIQEDG NQPFVSYRQA GDDYLLVDYG
HGSFDLNHRC RITALKKALN EEKRDRDSLS NGLIGMVGCG NSLMLYYDGL KVPQGKLIDY
LCDLENRLGD LSQAKMPSRL FKLPLTFESQ RQKDAMQRYM ETQRPYASYL PDNMDFVAKN
NALKMEELKN IYLTAKLMVV SVGFFMALPL ALPVDPRHRM NCPKMNPSRV YTPAGSVSWG
GSCMALYNVD SPGGYQMTGM TIPGVDILGS KKGYSADRPW LFEEFDQITF YQVSEAEYEK
QLALFNSGKY EHQWEEVIFD MAEHNRLLND TRDEVAAIRA RQRQAQAEMD KFEAQLLERW
ATEKAEKWVS QDAIEDLLQD PEIIAIEAPL NANVWKVEVK QAEKLEEGRV VVILEAMKLE
IAVRVESSAA GTTVEKVLVQ PGGPIEAGKP LMLVRKAACA DGYCLEKRPQ
//