ID M2SU68_COCSN Unreviewed; 801 AA.
AC M2SU68;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dethiobiotin synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCSADRAFT_40231 {ECO:0000313|EMBL:EMD60596.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD60596.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD60596.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445650; EMD60596.1; -; Genomic_DNA.
DR RefSeq; XP_007703642.1; XM_007705452.1.
DR AlphaFoldDB; M2SU68; -.
DR STRING; 665912.M2SU68; -.
DR GeneID; 19139675; -.
DR KEGG; bsc:COCSADRAFT_40231; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_010794_0_0_1; -.
DR OMA; KGWASRA; -.
DR OrthoDB; 5487177at2759; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000016934; 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; 3.40.50.300; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 801 AA; 88206 MW; 74A1949B4971E755 CRC64;
MARVPGGLWK RLVAVQVYGA NTGVGKTVFS TLLGAHFARR AGRTRWRVRY IKPVSTGPAD
EADDSYVQKY SGRSVSTLFK FNEAVSPHVA ARGADLIPSD ELISQTVFKT IQQEAKAVSG
EADAMGLAVI ETAGGVLSPG PSGTPQADIF RPLRLPSVLV GDHRLGGIAS TISAAESLVL
RGYDIDAVVC FNDQSKYENA EYLQEYFKNL GIAAFALPWI PNMQGIEAGT KEETDLMQGY
YNSQSSKEPI DQVAKRLLGR HSERLENLST MASRTNEAIW HPFTQHKHLK SADDILVFDS
AYGDYFQVKQ TGETSATHED RSALYPAFDG SASWWTQGLG HGNPRLALEA AHAAGRYGHV
MFAGATHEPA LELAEKMLND SQNPRLKKVF YTDNGSTATE VGIKMALRAA SKYYDWDSSK
ENIGVIGLKG SYHGDTIGAM DASEPCVFNE KVDWYRGRGF WFDFPTFKLK NGKWIVEPPE
NMESELGPTQ YFETQDAVFD LAARGRSERY EAYIEKTLDE LVRKQGRKFG ALVMEPVVLG
AGGMLFIDPL FQQTLVRVVR RYDFGNGSRA TRFPDENDVA WSGLPVMFDE VFTGLYRLGR
FSSASFLQTH PDISVNAKLL TGGLLPLSVT LASQSIFNAF WGDEKAEALL HGHSYTAHAV
GCHVANTSLQ TMQDASVGDE WKQYKKQWSS SNNNSTASWS MWSKGFVEDL SRHEQVGHVN
ALGSVLAVSL VDGHGSGYTS SAAVGLRDEL LRGSSEARQV QIHSRILGNV IYLMAGMLTT
RRHLEDVEKA FIEKLYVSSG R
//
