ID A1D1L6_NEOFI Unreviewed; 1237 AA.
AC A1D1L6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 28-JAN-2026, entry version 115.
DE SubName: Full=Urea amidolyase, putative {ECO:0000313|EMBL:EAW22309.1};
GN ORFNames=NFIA_009890 {ECO:0000313|EMBL:EAW22309.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22309.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
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; DS027688; EAW22309.1; -; Genomic_DNA.
DR RefSeq; XP_001264206.1; XM_001264205.1.
DR AlphaFoldDB; A1D1L6; -.
DR STRING; 331117.A1D1L6; -.
DR GeneID; 4590622; -.
DR KEGG; nfi:NFIA_009890; -.
DR VEuPathDB; FungiDB:NFIA_009890; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_002162_0_1_1; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000006702; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 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 InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:EAW22309.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006702}.
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 1153..1233
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1099..1133
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1237 AA; 135871 MW; 53988D11E2EA1A62 CRC64;
MDCLKTLLVA NRGEIAVRII KTAKKLNLRT IAIYTEPDAA SIHVHLADVA VLLSGSASKA
YIDGDQIIQI AKQNNANAII PGYGFLSENA DFARAVAAAG LVFVGPSPES IEAFGLKHTA
RELATKAGVP IVPGSPGLID NEDDAVEVAQ KLGYPVMLKA TAGGGGMGLL TCNSEAEVRK
SFATVKSRGE ALFKNAGVFI ERYYPASHHI EVQVFGNGDG KAIFIGEREC SIQRRHQKVI
EECPSPFVSR KPGLRKSLGE AAVRLAESIK YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
HGITELCYGM DLVELMLDQA DAQLSGKKGV EASFLEALPA ETPSGAAIEA RVYAENPTKD
FAPCPGTLQT VEWKEIPGSR IDTWIYRGIK VSANYDPLLA KVMYHSPDRQ QTILGMREIL
EKSRICGPPT NLDFLVKILE EEAFVAGNTL TRFLDNFQYT PSAIDVISGG AYTLIEDWPG
RPTIGRGFCH SGPMDPLAFR IANALVNNPV GLEALEITLS GPDLRFLGPA IISLCGAPIE
AKLDGETVPM WSRVKVAAGQ RLTIGKTTGN GCRAYLAVFG GFLNVPKWFG SKSTSPGVGV
GGYQGRQLSS GDLLTITSEI PEVNGDLRIP EHLIPDYPNH WELLAMPGPY DEGYLTPESI
EMLFETQWKI SHNAARGGIR LIGPKPQWAR SDGGEGGAHP SNVIEYGYAI GSVNWTGDDP
VIFPQDAPDF GGFVSSHTIV KADLWKLGQV KAGDTLKYRA VSLADALDAR RDMERFVDEL
VHCCKQGHGF HSVKALRGMP PEQTAETRGK GVVHRIEEQG NQPLVSYRQG GDDYLLIDYG
HGSFDLNHRC RVTALKKALN EGKEITFSNG LISMIGCGNS LMLYYDGMKL SQQRLISYLC
DLEAQLGDLS QAKMPSRLFR LPLTFESQRQ KDAIQRYMET QRPYASYLPD NMEFVAKNNA
FTKEEFENIF LTASLMVVSV GFFTALPLAL PVDPRQRMNC PKMNPSRVYT PAGSVSWGGS
CMALYNVDSP GGYQLTGMTI PGVDILGSKK GYSTDRPWLF EEFDQITFYR VSEEEYEKQL
ALFNSGQYEY QWEEVVFDMA EHNRLLQETR DEVAAIRARQ RQAQTEMDKI EAELLERWAK
EKTERGVSQD TIESLLQDPE IIAIEAPLNA NVWKVEVKQG DKLEENQVVV ILEAMKLEIA
VRVEPSTAGA TVEKVLAPPG EPIEAGKPLL LVRKVKT
//
