ID W2IL08_PHYPR Unreviewed; 864 AA.
AC W2IL08;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dethiobiotin synthase {ECO:0000313|EMBL:ETL34212.1};
DE Flags: Fragment;
GN ORFNames=L915_13626 {ECO:0000313|EMBL:ETK80794.1}, L916_13523
GN {ECO:0000313|EMBL:ETL34212.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL34212.1};
RN [1] {ECO:0000313|EMBL:ETK80794.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK80794.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETL34212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL34212.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL Submitted (NOV-2013) 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; KI687639; ETK80794.1; -; Genomic_DNA.
DR EMBL; KI674383; ETL34212.1; -; Genomic_DNA.
DR EnsemblProtists; ETK80794; ETK80794; L915_13626.
DR EnsemblProtists; ETL34212; ETL34212; L916_13523.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR Proteomes; UP000053864; 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; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETL34212.1"
SQ SEQUENCE 864 AA; 95162 MW; A6D04066545D5559 CRC64;
CVPHQLIVRT SFTIFPVRTV FRLSLVSTNF HRLTRNQLHD ASIIARTQSP IHCLPLKPSM
MLSKALRRPS LHRPVASVMK YHIGVRETQL GADALSKQKQ QLRTQGASSV NLDTPVFQVF
GSNTDIGKTI VSAGICRSAA TIAASNGGRI EYIKPLQTGT DDDIPGSFPG DASFIEKHAL
LKDQKQGDLQ CSTLFSWKNP VSPHLAAQME GYTITDEKLL ELLSDKLKAI NQVNGAKAAD
SLVLVETAGG VCSPSASMRF QVDVYRGMRL PVVLVGDGKL GGISTTMSAL ETLLIRGYDV
AAICLIEQDG LDNKAALEPR TSELGIPIFT MNAVPPMPEP LNKWFEKHDK VFADVNKALK
SFHKTRLESF KRMEERAEQV FWWPFTQHKK AGGLSMIDSA HGDEFSVYRP DSNTVEPLFD
ACASWWTQGV GHGNSKMATA LAYAAGRYGH VMFPENAHEP ALQLSEKLLA SVGKGWASRV
YYSDDGSTAV EVALKMAFRK YVLDHKLEYG EFMSDEATGS KMVTLAQANC YHGDTLGVMN
VAEKSVFNEK QHPWYRPEGV FLKVPTMALR DGEYVVSIDP EIAGSAKTEE KLPSLNAAFD
SKRDQSSLAN VYRKHVSKMI DETEEKNVRV GSALIEPVLM GSGGMFLVDP LYQRMLVQEC
RARKIPVIYD EVFSGWWRLG VESARDLLDV DPDIACYAKL LTGGVVPMAA TLASEEVFNT
FYADSKGEAL LHGHSFTAYP MGCAAAVTAL DMYEIFNNAS GPIKDATRTY WDVNALKELS
SRSYIERTFA IGTVACVELA SENAGYASTE AAEFIHVLRK NGVYARSLGN VLYMMCSPLT
TQEDCSKYLG TLINQIEILQ AKKR
//
