ID   Q6NEX3_CORDI            Unreviewed;       423 AA.
AC   Q6NEX3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, 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=DIP2136 {ECO:0000313|EMBL:CAE50666.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE50666.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE50666.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248360; CAE50666.1; -; Genomic_DNA.
DR   RefSeq; WP_010935606.1; NC_002935.2.
DR   AlphaFoldDB; Q6NEX3; -.
DR   STRING; 257309.DIP2136; -.
DR   KEGG; cdi:DIP2136; -.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:CAE50666.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198};
KW   Transferase {ECO:0000313|EMBL:CAE50666.1}.
FT   DOMAIN          53..413
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   423 AA;  46909 MW;  BD8FD73B6CF0EA58 CRC64;
     MNNKKETPQA APAQRKRTRR IFDQSDKLKN VLYEIRGPVT AEAEAMELDG HRILKLNTGN
     PAIFGFEAPD VIMRDMIASL PTSQGYSTSK GIIPARRAIV TRYEVIPGFP AFDVDDVYIG
     NGVSELITMT TQALLNNGDE VLIPMPDYPL WTAATSLAGG KPVHYLCDEE DDWNPSIEDI
     KSKITERTKA IVVINPNNPT GAVYSKEVLQ KIVDVAREHD LLILADEIYD RILYDGAVHT
     NIAALAPDLL CITFNGLSKA YRVAGYRAGW MIVTGPKNNA RGFIEGLDLL SGTRLCANVP
     GQHAIQVALG GRQSIYDLTG QGGRLLEQRN VTWEKLNAIP GVSCVKPMGA LYAFPKLDLE
     YYDIKDDAQL MLDLLRQEKI LMVQGTGFNW DKPDHFRVVT LPWASQLSEA MDRLGNFLAS
     YKQ
//