ID   Q8NLU2_CORGL            Unreviewed;       419 AA.
AC   Q8NLU2;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Cgl2844 {ECO:0000313|EMBL:BAC00238.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627 {ECO:0000313|EMBL:BAC00238.1, ECO:0000313|Proteomes:UP000000582};
RN   [1] {ECO:0000313|Proteomes:UP000000582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
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}.
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DR   EMBL; BA000036; BAC00238.1; -; Genomic_DNA.
DR   RefSeq; NP_602037.1; NC_003450.3.
DR   AlphaFoldDB; Q8NLU2; -.
DR   STRING; 196627.cg3149; -.
DR   KEGG; cgl:Cgl2844; -.
DR   PATRIC; fig|196627.13.peg.2777; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   OrthoDB; 9763453at2; -.
DR   BioCyc; CORYNE:G18NG-12461-MONOMER; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0004069; F:L-aspartate: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:BAC00238.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000582};
KW   Transferase {ECO:0000313|EMBL:BAC00238.1}.
FT   DOMAIN          48..410
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   419 AA;  46749 MW;  57DFDE87850F30E4 CRC64;
     MGADQAARPT RRTTRRIFDQ SEKMKDVLYE IRGPVAAEAE RMELDGHNIL KLNTGNPAVF
     GFDAPDVIMR DMIANLPTSQ GYSTSKGIIP ARRAVVTRYE VVPGFPHFDV DDVFLGNGVS
     ELITMTTQAL LNDGDEVLIP APDYPLWTAA TSLAGGKPVH YLCDEEDDWN PSIEDIKSKI
     SEKTKAIVVI NPNNPTGAVY PRRVLEQIVE IAREHDLLIL ADEIYDRILY DDAEHISLAT
     LAPDLLCITY NGLSKAYRVA GYRAGWMVLT GPKQYARGFI EGLELLAGTR LCPNVPAQHA
     IQVALGGRQS IYDLTGEHGR LLEQRNMAWT KLNEIPGVSC VKPMGALYAF PKLDPNVYEI
     HDDTQLMLDL LRAEKILMVQ GTGFNWPHHD HFRVVTLPWA SQLENAIERL GNFLSTYKQ
//