ID A2V7M6_STRGR Unreviewed; 403 AA.
AC A2V7M6;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=NCTC13033_03539 {ECO:0000313|EMBL:SQA23806.1};
OS Streptomyces griseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1911 {ECO:0000313|EMBL:BAF46972.1};
RN [1] {ECO:0000313|EMBL:BAF46972.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO13350 {ECO:0000313|EMBL:BAF46972.1};
RX PubMed=17158669; DOI=10.1128/JB.01708-06;
RA Suzuki H., Ohnishi Y., Horinouchi S.;
RT "Arylamine N-acetyltransferase responsible for acetylation of 2-
RT aminophenols in Streptomyces griseus.";
RL J. Bacteriol. 189:2155-2159(2007).
RN [2] {ECO:0000313|EMBL:SQA23806.1, ECO:0000313|Proteomes:UP000251334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13033 {ECO:0000313|EMBL:SQA23806.1,
RC ECO:0000313|Proteomes:UP000251334};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; AB280932; BAF46972.1; -; Genomic_DNA.
DR EMBL; UAVD01000028; SQA23806.1; -; Genomic_DNA.
DR RefSeq; WP_012379289.1; NZ_UAVD01000028.1.
DR AlphaFoldDB; A2V7M6; -.
DR STRING; 1911.GCA_001715295_02064; -.
DR GeneID; 6210171; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000251334; Unassembled WGS sequence.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:BAF46972.1};
KW Transferase {ECO:0000313|EMBL:BAF46972.1}.
FT DOMAIN 34..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 44255 MW; 1001E69B690C6BD9 CRC64;
MQVIQSTKLS NVCYEIRGPV LEEAMRLEAA GQRILKLNTG NPAAFGFECP PEILEDILRN
VAGAHGYGDA KGLLSARRAV VQHYQTKGIE LDVEDIYLGN GVSELIQMSM QALLDDGDEV
LVPAPDYPLW TASVSLAGGT AVHYRCDEQA DWMPDLADVE RKITDRTKAL VIINPNNPTG
AVYDDEMLRG LTEIARRHNL IVCSDEIYDR ILYDGATHTP TAALAPDLMV LTFNGLSKNY
RVAGYRSGWM AVCGPKAHAT SYIEGLTILA NMRLCANMPS QHAVATALGG RQSIQDLVLP
GGRILEQRDA AYDLLTSIPG VSCVKPKGAL YLFPRLDPKV YKIKDDRQMV LDLLRAEKIM
VVQGTGFNWP EPDHFRIVTL PTVEDLTDAV TRIGTFLDGY GQP
//
