ID A0A124IFM3_9ACTN Unreviewed; 403 AA.
AC A0A124IFM3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=AQJ91_07185 {ECO:0000313|EMBL:KUO21906.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO21906.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO21906.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO21906.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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}.
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:KUO21906.1}.
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DR EMBL; LMXB01000021; KUO21906.1; -; Genomic_DNA.
DR RefSeq; WP_067017570.1; NZ_KQ949077.1.
DR AlphaFoldDB; A0A124IFM3; -.
DR STRING; 909626.AQJ91_07185; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
DR GO; GO:0004021; F:L-alanine: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:KUO21906.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW Transferase {ECO:0000313|EMBL:KUO21906.1}.
FT DOMAIN 34..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 44227 MW; 3332143C4DF634F3 CRC64;
MQVIQSTKLA NVCYEIRGPV LEEAMRLESA GHRILKLNTG NPAAFGFECP PEILEDILRN
VSSSHGYGDA KGLLAARRAV VMHNQTLGIE TDVEHVFIGN GASELIVMAM QGLLDDGDEV
LVPSPDYPLW TAAVSLSGGT AVHYRCDEQS DWMPDLADVE RKVTDRTKAI VIINPNNPTG
AVYDEAMIKG LTDIARRHNL LVCSDEIYDK ILYDGATHTP TAAIAPDLLT LTFNGMSKAY
RVAGYRVGWM SISGPRAHAD SYIEGLTILA NMRLCANMPG QHGVVAALSG RQTINDLVLP
GGRLKEQMDT AYELLTQIPG VSCVRPKGAL YLFPRLDPNV FKIRDDRQLV LDLLRREKIM
VVQGTGFNWS EPDHFRVVTL PTVGDLRDAV TRIGNFLDGY SQP
//