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
//