ID A0A0F0LW52_9MICO Unreviewed; 408 AA.
AC A0A0F0LW52;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN Name=alaA {ECO:0000313|EMBL:KJL35636.1};
GN ORFNames=RR49_02395 {ECO:0000313|EMBL:KJL35636.1};
OS Microbacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL35636.1, ECO:0000313|Proteomes:UP000033451};
RN [1] {ECO:0000313|EMBL:KJL35636.1, ECO:0000313|Proteomes:UP000033451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL35636.1,
RC ECO:0000313|Proteomes:UP000033451};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL35636.1}.
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DR EMBL; JYIY01000078; KJL35636.1; -; Genomic_DNA.
DR RefSeq; WP_045248292.1; NZ_JYIY01000078.1.
DR AlphaFoldDB; A0A0F0LW52; -.
DR STRING; 400772.RR49_02395; -.
DR PATRIC; fig|400772.4.peg.2407; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000033451; 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:KJL35636.1};
KW Pyruvate {ECO:0000313|EMBL:KJL35636.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033451};
KW Transferase {ECO:0000313|EMBL:KJL35636.1}.
FT DOMAIN 38..397
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 408 AA; 44957 MW; EC52877FE00329FD CRC64;
MSPLRPLDQS RKLKDVLYEI RGQALVEADR LEADGHRILK LNTGNPATFG FEAPYQIVRD
MIEAVPHAHG YSESRGILSA RRAIVSRYEQ VPGFPHVDPD DVYLGNGVSE LITMTMQALL
DEGDEVLIPS PDYPLWTAMT SLGGGSPVHY RCDEQNGWQP DIDDIRAKVT PRTKAIVVIN
PNNPTGAVYS PELLTQIVEV AREHSLLLLA DEIYDRILFD DAVHTPLATL APDLLCLTFN
GLSKTYRVAG YRSGWLVITG PTSHAAGFLE GITLLASTRL CPNVPAQYAV QAALSGVQSI
DALIAPAGRL HEQRDAAWQA LESIPGVSCV KPAGALYAFP RLDPEVHEIH DDAKFVYDFL
VAEHVLLVQG TGFNWPDPDH FRIVTLPETR VLVEAIERLG NFLSSYRQ
//
