ID A2QZM5_ASPNC Unreviewed; 1294 AA.
AC A2QZM5;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Contig An12c0160, genomic contig {ECO:0000313|EMBL:CAK46257.1};
DE EC=3.5.2.9 {ECO:0000313|EMBL:CAK46257.1};
GN ORFNames=An12g05460 {ECO:0000313|EMBL:CAK46257.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK46257.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK46257.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the oxoprolinase family.
CC {ECO:0000256|ARBA:ARBA00010403}.
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DR EMBL; AM270272; CAK46257.1; -; Genomic_DNA.
DR EnsemblFungi; CAK46257; CAK46257; An12g05460.
DR VEuPathDB; FungiDB:An12g05460; -.
DR HOGENOM; CLU_002157_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR InterPro; IPR049517; ACX-like_C.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1.
DR PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR Pfam; PF19278; Hydant_A_C; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR Pfam; PF02538; Hydantoinase_B; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CAK46257.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 11..224
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 244..538
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 634..724
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
FT DOMAIN 743..1255
FT /note="Hydantoinase B/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF02538"
FT REGION 1247..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1294 AA; 140237 MW; 3C4851D648CF4CFD CRC64;
MPSLEPRQKL RISIDRGGTF TDCICKVLGQ EDIVVKILSV DPKNYDDAPT EAIRRVLEIY
YGRSIPRGTG LDTKDIESIR MGTTVATNAL LERKGERTAL LITEGFKDLL EIGNQSRPFM
FDLSIRRPET LYSDVFEVDE RVTLRNCTDT DLRSMDLSSP PVLRELTGTS GETVQIIKTL
DLEPVEVYLR KIYTDGYRSI AVCLMHAYTF PDHELQIREL AQQIGFENVS LSHAVSQRTK
IVPRGNSAVI DGYLTPTIER YLKQFLTSFP NISKSDTKLE FMQSDGGLVP AHRLSGLHSI
LSGPAGGVVG YARTCYDEVS KAPLIGFDMG GTSTDVSRYD GTLDHIFETT TAGISMQTPQ
LNINTIAAGG GSILFWRDGL MSVGPESASS DPGPACYRKG GPLTITDANL ALGRLIPDYF
PSVFGPNENE PLDRDVVISK FEDMTAAINL DTGKSLSWEE VAQGFLDVAN SAMCGPIRSL
TEARGYDTTK HQLASFGGAG GQHACAIAEL LGIQKVLIHK HSSILSAYGI GLADVVQEGQ
RPCAKAYEPY NLPTILSDLE DLAQATKDLL GNDGILNVDV DRFLNMRYDG SETTIMIAVD
QNHNMLPTFV NAHHQQFGFT PTDRKVFVDS IRVRAIGRGS FAAPSPDVPA SVPEKLSIPS
HKSPTAEATN RVYFNELGWT DTPVYILKSI PLGQKVSGPA LVVDETQTIL VGPGSSATSE
QDKLILDINV SGKGLSVATD TIDPVQLSVF RHRFMSVAEQ MGRVLQQVSV SANIKERLDF
SCAVFSPDGS LVANAPHVPA MIGSMAFAVK GQIEEWKGRL KPGDVLLSNA PEYGGTHLPD
LTVITPVFDA QGRDIIFWTA SRGHHADIGG ILPGSMPPSS KELGQEGALF KSFLLIRDGT
LDEVGLSRML CDEPARYPGS SGTRRYQDNV TDLKAQVAAN HCGIRLIHQL IEEYSMKVVQ
VYMKAIQSSA ELAIRNLFKR LARQFHQTEL KEVDYMDDGT PICLKITLDE AEGSAVFDFT
GTGPQVYAIT HSSIIFALRC IVDSDIPLNH GCLAPVTVHV PKPSLLNPAP TAAVCAGNVL
TSQRIVDVIF KTLRVCAASQ GCMNNFSFGT DDFGYYETIA GGSGAGPSWS GTNGVHTNMT
NTRITDPESL ERRYPVLLRR FCFRGGSGGD GKYRGGDGVV RDVEFRIPMT ASILSERRVV
KPFGMDGGGN GCCGRNLWIK GEDGEIMSIG GKNSVEMGAG DRLVIETPGG GGYGRKDDRD
GDSKVEGDQA KVNKGFVPIA NGSVEAARSL AEQV
//
