ID D7BUH1_STRBB Unreviewed; 397 AA.
AC D7BUH1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspC2 {ECO:0000313|EMBL:ADI11720.1};
GN OrderedLocusNames=SBI_08602 {ECO:0000313|EMBL:ADI11720.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11720.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI11720.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11720.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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; CP002047; ADI11720.1; -; Genomic_DNA.
DR RefSeq; WP_014181169.1; NC_016582.1.
DR AlphaFoldDB; D7BUH1; -.
DR STRING; 749414.SBI_08602; -.
DR KEGG; sbh:SBI_08602; -.
DR PATRIC; fig|749414.3.peg.8848; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:ADI11720.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ADI11720.1}.
FT DOMAIN 38..388
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 43022 MW; 18406889A8F3EE83 CRC64;
MNSTLDLAEP AARLADIKPS PIRAIFDRAS ELERAGERVI HLEIGRPDFD TPEVAKQRAA
QAIADGKVHY GPNAGQPELR AAISRYLDRR HNLTYSPDDE VLVTIGANEA VFLAIMAFCG
PGDEVVIPVP AWSAYVACVR LAGATPVILP LSADDGYQVN PDALAAVMTE RTRMVVLCTP
HNPTGAVTDP KRLAGVADVV RDTRALVLSD EIYAELVYGG QRHISPASVA DLRHRTLVVG
GFAKAYAMDG WRLGWLAGPK ELVRPALRIR QFTTICPTTF AQLGGAAALD EAGAEREAMR
QEFERRRNVA LEVLAQQDVL SPGEPGGAFY LYLSYPERLG PSDELAWRLL EEQHVAVVPG
TAFDSDGGKH ALRISYACGI DDLREGLNRL VATVQSN
//
