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Database: UniProt
Entry: A0A124IFM3_9ACTN
LinkDB: A0A124IFM3_9ACTN
Original site: A0A124IFM3_9ACTN 
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
//
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