ID W2RSV9_9EURO Unreviewed; 840 AA.
AC W2RSV9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Dethiobiotin synthase {ECO:0000313|EMBL:ETN38809.1};
GN ORFNames=HMPREF1541_06848 {ECO:0000313|EMBL:ETN38809.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN38809.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN38809.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN38809.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-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; KB822722; ETN38809.1; -; Genomic_DNA.
DR RefSeq; XP_008719398.1; XM_008721176.1.
DR AlphaFoldDB; W2RSV9; -.
DR STRING; 1220924.W2RSV9; -.
DR GeneID; 19974187; -.
DR VEuPathDB; FungiDB:HMPREF1541_06848; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_010794_0_0_1; -.
DR InParanoid; W2RSV9; -.
DR OrthoDB; 5487177at2759; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000030752; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 840 AA; 91240 MW; 7E8EC26AF3B1D20A CRC64;
MLWRDLKAWQ VYGANTDVGK TIVSTVLCKA LQRRAPSNGV LYLKPVSTGP LNEADDRHIS
RFAPGVVSKC LSQFSEPVSP HLAAKIDSVD KALTDDSTIV SKIKRQLNKQ LEQGTRYALL
ETAGGILSPG PSGSLQADLY RPLRLPTLLI GDHKLGGIAT TISAFESLHL RGYDVDSLLL
FDDPQWGNFA YLQDHFAKHD VQAVALPLPP PRRKTPKDDE QAMAEYYEQC STSPGINTLL
ESLNQKHFSR VSKLTSLPSH ADSIIWHPFR QHGLPQNIIA IDSAYGDTFE VYNQEADPAV
AASQVGTTGL NTGSSGTQAK PLTTPLFDAS ASWWTQGFGH GNPELSLTAA HAAGRYGHVM
FGSAVHEPAL DLCYNLLETL RSPRLTRVFF TDNGSTGMEV AVKMALRATS LRYGWTKNDG
GRPVEILGLK GSYHGDTIGV MNASEPSVFN EAVDWYQPWG TWFDPPSVLL SKGKWHVSVP
SSFLEPGSTK TWYFQHMASL FDFSSRETHA KFYRDFITKA LRSLCHDQGR RFGALVMEPI
IMGAGGMIFV DPLFQHTLIT TIRENPSLIN PKYQPSSNPD PADWSGLPLI ADEVFTGLYR
LGRSSSSSFL SPDPLSPTPM SVSTAPDVSV HAKLLTGGIL PLALTTASNS IFNAFLSDSK
TDALLHGHSY TAHPIGCSVA NHALKEMERL DTSGNSDWQA YRSPWAAAPS IPDLSSSSST
ANPSPSSSTV NTPYSFFSPH LLTQLSHHPL LSGLWSLGTV LALTLKSTEG TSGGYASNAT
ASLQSRLLTT LDEKTGEGIH ARVLGDVIYF MCSLTTKPDA AERLGSVLLR ALDGELEDQE
//
