GenomeNet

Database: UniProt
Entry: A0A0X3SDH1_9ACTN
LinkDB: A0A0X3SDH1_9ACTN
Original site: A0A0X3SDH1_9ACTN 
ID   A0A0X3SDH1_9ACTN        Unreviewed;       402 AA.
AC   A0A0X3SDH1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=ADL25_22235 {ECO:0000313|EMBL:KUJ38955.1};
OS   Streptomyces sp. NRRL F-5122.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ38955.1, ECO:0000313|Proteomes:UP000054048};
RN   [1] {ECO:0000313|Proteomes:UP000054048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
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:KUJ38955.1}.
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; LMWH01000228; KUJ38955.1; -; Genomic_DNA.
DR   RefSeq; WP_059129511.1; NZ_LMWH01000228.1.
DR   AlphaFoldDB; A0A0X3SDH1; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000054048; 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:KUJ38955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW   Transferase {ECO:0000313|EMBL:KUJ38955.1}.
FT   DOMAIN          34..392
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   402 AA;  44415 MW;  E1CF346FA0CDCE7D CRC64;
     MEFRQSSKLS EVCYEIRGPV IEHANALEEA GHSVLRLNTG NPALFGFEAP EEILQDMIRM
     LPQAHGYTDS RGVLSARRAV AQRYQERGLD VDVDDVFLGN GVSELVSMAV QALLEDGDEV
     LIPAPDFPLW TAVTTLAGGK AIHYLCDEQA DWYPDLDDMA AKITDRTRAV VIINPNNPTG
     AVYPKEVIEG ILDLARRHGL MVLADEIYDQ ILYDGAVHHS AAALAPDLVV LTFCGLSKTY
     RVAGFRSGWL VVTGPKQHAR NYLEGLTMLA SMRLCANAPA QYAIQAALGG RQSIHELTAP
     GGRLREQRDR AWERLNEIPG VSCVKPKGAL YAFPRLDPKV HPIHDDEKFV LDLLLREKIQ
     VVQGTGFNWP APDHFRILTL PHADDLEAAI GRIGRFLGGY RQ
//
DBGET integrated database retrieval system