ID E6PBP8_AJEC8 Unreviewed; 822 AA.
AC E6PBP8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Bifunctional dethiobiotin synthetase/adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:DAA33944.1};
DE EC=2.6.1.62 {ECO:0000313|EMBL:DAA33944.1};
DE EC=6.3.3.3 {ECO:0000313|EMBL:DAA33944.1};
DE SubName: Full=Onanonoxo-7-onima-8-eninoihtemlysoneda {ECO:0000313|EMBL:QSS57847.1};
GN Name=bioDA {ECO:0000313|EMBL:DAA33944.1};
GN ORFNames=I7I53_12153 {ECO:0000313|EMBL:QSS57847.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|EMBL:DAA33944.1};
RN [1] {ECO:0000313|EMBL:DAA33944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:DAA33944.1};
RX PubMed=20713166; DOI=10.1016/j.fgb.2010.08.004;
RA Magliano P., Flipphi M., Sanglard D., Poirier Y.;
RT "Characterization of the Aspergillus nidulans biotin biosynthetic gene
RT cluster and use of the bioDA gene as a new transformation marker.";
RL Fungal Genet. Biol. 48:208-215(2011).
RN [2] {ECO:0000313|EMBL:QSS57847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS57847.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) 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}.
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DR EMBL; BK007850; DAA33944.1; -; Genomic_DNA.
DR EMBL; CP069107; QSS57847.1; -; Genomic_DNA.
DR AlphaFoldDB; E6PBP8; -.
DR VEuPathDB; FungiDB:I7I53_12153; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000663419; Chromosome 6.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:DAA33944.1}; Ligase {ECO:0000313|EMBL:DAA33944.1};
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:DAA33944.1}.
FT REGION 309..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 90577 MW; 9C4790D7601649F1 CRC64;
MACVGAFLSK HLLTYQVCGA NTNVGKTVFS SLLYKAHALS KPKTNHWYLK PVSTGPECDR
DDRHISRFAK HVSIKCLYIF DQPVSPHLAA AGKQCPGDGE IVEAVSQTLH GWAQYGRGLA
LVETAGGVLS PGPNGTLQSD LYRPLRLPVI LVADSRLGGI SSSIAAFESL SLRGYDVHAV
AVLEDSFYQN HTYLEEFFLS KRNIPVLTVP QPPPKQLTGD DSVAADDEQK MSRYYEEQAI
RLLTEVHGPR SSFLDRLSEK HHSRISELES MSARAHSSIW YPFTQHQSLA PKDIMVIDSA
YGDCFQTSTV NSTESGSEPT AANTEPSQKN TSNLLRPTFD GSASWWTQCL GHGNPELSLE
AAYAAGRYGH VILPGAIHEP ALSLAESLIK MINNPRLKRA FYSDNGSTGM EVAVKMALRV
ACKRYNWGSS KEDIEILGLR GSYHGDTIGT MDLSEPSIYN KKVEWYRGRG HWFNFPTVKM
LRGRWIIEIP QELKGSLGNN TEFPTRQSIF DLAQRKKSVA RQRYYTYIKR SLEKLICQDG
RKFGALIMEP VILGAGGMLF ADPLFQQTMV EVVRENPALF GGGHAPPPSS SDRTWSGLPV
VFDEVFTGLY RLGRASSASF LDTHADISVH AKLLTGGLVP LCITLASEDI FDAFCTPHKV
DALLHGHSYT AHPVGCRVAE ASLRMLTTKN AERCQQMQLR DQPHHQPHNQ PPVETGVDLP
EQLRHVWSSW SDQLVLDLSH SEQVEAVFAL GTVLSISLRS QDGSGYGSNA AAGLQQRLGE
TNADGFNIHC RVLGNVLYLM CDLTSGVEQL ARIEKAVCTA LL
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