ID A2QQ54_ASPNC Unreviewed; 1318 AA.
AC A2QQ54;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Contig An08c0030, genomic contig {ECO:0000313|EMBL:CAK39813.1};
DE EC=3.5.2.9 {ECO:0000313|EMBL:CAK39813.1};
GN ORFNames=An08g01320 {ECO:0000313|EMBL:CAK39813.1};
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:CAK39813.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK39813.1, 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; AM270158; CAK39813.1; -; Genomic_DNA.
DR RefSeq; XP_001392250.1; XM_001392213.1.
DR EnsemblFungi; CAK39813; CAK39813; An08g01320.
DR GeneID; 4982446; -.
DR KEGG; ang:An08g01320; -.
DR VEuPathDB; FungiDB:An08g01320; -.
DR HOGENOM; CLU_002157_0_1_1; -.
DR OrthoDB; 674at2759; -.
DR Proteomes; UP000006706; Chromosome 8R.
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:CAK39813.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 9..229
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 248..543
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 551..734
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
FT DOMAIN 747..1280
FT /note="Hydantoinase B/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF02538"
SQ SEQUENCE 1318 AA; 142698 MW; 3A272A9A60B0E5B5 CRC64;
MSSSKLNIKI AIDRGGTFTD CLGIVDGRKE DIVVKLLSQD PANYADAPIE GIRRILEQAT
GKCFPRDQKL TTSDFGGVSI RMGTTVATNA LLERKGERVA LLITKGFKDA LRIGTQSRPK
LFALNIQRPD VLYEEVVEID ERVTIEGYQQ DPAPDKESLE AALETDPYLK KGVSGEVIRV
LEPLDEAKIR QSLQKLYSEG FRSIAVCLVH SYTFQEHELA IERIANEIGF TQISLSSQLL
PMIKMTSRGA SATADAYLTP VIQRYIQGFR SGFQDKLQSS DTRCEFMQSD GGLVNFQKFS
GLRAILSGPA GGVVGYAGTS FDPEDRKPVI GFDMGGTSTD VSRYDGKLEH TFENTISGVT
VMAPQLDINT VAAGGGSILF WRHGLFVVGP ESAGAHPGPA CYRKGGPLTV TDANLFLGRL
LPEYFPKIFG PNENEPLDIE VTCQKFTELA DKINAETGHK KTPEEIALGF IQVANESMAK
PIRALTEARG YDTAAHNLAC FGGAGGQHAC AIASSLSIKT VIVHCYSSIL SAYGMALADV
VHEAQEPASG ALTANAMETI NGRIEALKAK VTEALTVDGI EETRIQYEVY LNLRYQGTDN
TLMVLRPDNG DFGEAFIEEH QREFSFTFPG RNILVEDIRV RGVGKAISVP PEAPQPELRS
ITTSVIGEQS QNDSTEVYFA GVGRVTTPVF FLEHLKPGSF IQGPAMIIDK TQTIVVEPHA
SATILSRHVI LNVQSVKNQF DNATVVDPIK LSIFGHRFMS VADQMSRMFQ KTSVSTNIKE
RLDFSCAVFS PDGKLVANAP NVPVHLGSME YAVRYQHEQY GGDLKPGDHI LTNHPLAGGT
HLPDITIITP VWDQQGSKII FYVASRGHHA EIGGIAPGSM PSDSKMLYEE GAMTLGFKVV
SQGRFDEDMV RKFLYDEPAS YPGCSGTRTY KDNVSDLKAA IAANQKGAQL LEGLVQENTL
DVVHFYMNAI KKNAETAVRD LLKTIGKKAA GQPLRFSDFM DDGTEIRLEI RIDAETGSAE
FDFTGTGRET FNCLNAPKAI AHSAIIYSLR ALIDVDIPLN QGCLAPINVI IPSGTLINPS
GYAAVCAGNP ITSQRITDVV LGAFQACAAS QGCCNIISFG MGGLDESGND IPGFGVGETI
CGGSGAGPTW HGTSGVHVHM TNTRITDAEV YELRYPVILR QFSIRKGSGG KGLYRGGDGV
IRELEFRIPL SASMLSERRV YRPYGLAGGE SGQPGLNLYV KKELDGTERV INIGGKMELK
VQPGERIIIH TPGGGGWGTP AEEDPIPIRS SNNLEANRVV FEARGSVHRF SATAEAAL
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