ID A0A0A2VXV0_BEABA Unreviewed; 727 AA.
AC A0A0A2VXV0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000313|EMBL:KGQ11015.1};
GN ORFNames=BBAD15_g3599 {ECO:0000313|EMBL:KGQ11015.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11015.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ11015.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11015.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-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: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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:KGQ11015.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANFO01000251; KGQ11015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VXV0; -.
DR STRING; 1245745.A0A0A2VXV0; -.
DR HOGENOM; CLU_380800_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:EnsemblFungi.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:1902117; P:positive regulation of organelle assembly; IEA:EnsemblFungi.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR CDD; cd06454; KBL_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR HAMAP; MF_00627; Thr_dehydrog; 1.
DR InterPro; IPR011282; 2am3keto_CoA_ligase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR004627; L-Threonine_3-DHase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01822; 2am3keto_CoA; 1.
DR NCBIfam; TIGR00692; tdh; 1.
DR PANTHER; PTHR13693:SF103; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:KGQ11015.1}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 398..724
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 727 AA; 79509 MW; 1F665F414A0223DC CRC64;
MREDFYQQLT SQLETARAEG LFKEERIITS AQQADITVAD GSHVINFCAN NYLGLANHPQ
LIEAAKHGMD KHGFGMASVR FICGTQDSHK QLESKLADFL GTDDAILYSS CFDANGGLFE
TLLGPEDAII SDALNHASII DGVRLCKAQR YRYANNDMQE LEDRLKEARA AGARHVMIAT
DGVFSMDGVI ANLQGVCDLA DKYNALVMVD DSHAVGFVGA NGRGTHEYCD VMDRVDIITG
TLGKALGGAS GGYTAGRKEV IEWLRQRSRP YLFSNSLAPA IVSASIKVLE MLESGEELRE
RLWSNARLFR EKMSAAGFTL AGADHAIIPV MLGEAVVAQN FARELQKEGI YVTGFFYPVV
PKGQARIRTQ MSAAHTPEQI ERAVDAFTRI AKLKAEEGIW MTDAPKPEMG HNDLLIKIRK
TAICGTDVHI YNWDEWSQKT IPVPMVVGHE YVGEVVGIGQ EVKGFKIGDR VSGEGHITCG
HCRNCRGGRT HLCRNTTGVG VNRPGCFAEY LVIPAFNAFK IPDNISDDLA SIFDPFGNAV
HTALSFDLVG EDVLVSGAGP IGIMAAAVAK HVGARNVVIT DVNEYRLELA REMGITRAVN
VSKESLQDVM SELGMTEGFD VGLEMSGAPP AFRTMLDTMN HGGRIAMLGI PPSDMSIDWT
KVIFKGLFIK GIYGREMFET WYKMAALIQS GLDLSPIITH RFSIDEFQKG FDAMRSGQSG
KVILSWD
//
