ID I7ZLB5_ASPO3 Unreviewed; 798 AA.
AC I7ZLB5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:EIT72754.1};
GN ORFNames=Ao3042_01208 {ECO:0000313|EMBL:EIT72754.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT72754.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT72754.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT72754.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746}.
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:EIT72754.1}.
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DR EMBL; AKHY01000214; EIT72754.1; -; Genomic_DNA.
DR AlphaFoldDB; I7ZLB5; -.
DR HOGENOM; CLU_010794_0_0_1; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002812; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03109; DTBS; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EIT72754.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIT72754.1}.
SQ SEQUENCE 798 AA; 87809 MW; 65FFCFF93EAECB35 CRC64;
MSPVGAVLWR SLRAHQVYGA NTDVGKTIVS TVLCNAVQRL KSQDQAAFLK PVSTGPLDDA
DDRHIQRHAA GTLTKCLYQF DEPVSPHIAA QQKKFTIPRD DDIVASVHKT LSDWAGSGVN
FALVETAGGV HSPGPNGNSQ ADLYRPLRLP IVLVADSRLG GISSSISAYE SLLLRGYDVH
SVLLFRDEYY KNHEYLLNYF QKKCIPLVPL PSPPPKPSVQ DADSLARDEE AMTTYYGRVA
QETDVASLLQ QLSSKNAERI DRLESMASRA HDTIWYPFTQ HHGMEAKDIT PIDSAYDDYF
QTFVGSDESQ HENKLRATFD GSASWWTQGL GHGNPSLALS AAYAAGRYGH VMFPGNIHEP
ALSLAELLIE SIGNPRLRKV FYTDNGSTGM EVAVKMGLRA ACDRYGWDAS QEQISILGLK
GSYHGDTIGV MDCSEPSTFN KKVEWYRGRG YWFDFPQVKM SQGVWKVEIP ENLRESLGSG
LEFSSLDEIF DMEERLQSAA GKRYQDYIRN TIQDLVHQHR MKFGSLIMEP IILGAGGMLF
CDPLFQRCLV EVVRGHPELF DTSAAKSAKD HPVATSWSGL PVIFDEVFTG LYRLGRKSSA
SFLQVDSDVS VNAKLLTGGL LPLCTTMASN EIFQAFSSPE KSDALLHGHS YTAHAVGCQV
AVDSLQTMMQ MENSGSWDGY RQDWKPTRSD SPATLSARDS LDIWSVWSHG LVSDLSHAPS
VDGVFAIGTV LSISLKDVQG GGYTSTAARG LQQRLSTSDG KFNVHSRVLG NVLYLMSSVT
SQPEALRSIE GLLREALL
//
