ID   U3GZY8_9CORY            Unreviewed;       396 AA.
AC   U3GZY8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=CARG_09025 {ECO:0000313|EMBL:AGU15902.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15902.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU15902.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15902.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(2013).
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; CP006365; AGU15902.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3GZY8; -.
DR   STRING; 1348662.CARG_09025; -.
DR   KEGG; caz:CARG_09025; -.
DR   PATRIC; fig|1348662.3.peg.1782; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000016943; Chromosome.
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:AGU15902.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016943};
KW   Transferase {ECO:0000313|EMBL:AGU15902.1}.
FT   DOMAIN          26..387
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   396 AA;  43969 MW;  77B88BA2B9B75947 CRC64;
     MKDVLYEIRG PVSAEAERLE LDGHRILKLN TGNPAVFGFE APDVIMRDMI AALPTSQGYT
     TSKGIIPARR AIVTRYEVIE GFPYFDVNDV FLGNGVSELI SMVTQALLND GDEVLIPMPD
     YPLWTAATSL AGGKPVHYLC DEEDDWNPSI EDIRAKVTDK TKAIVVINPN NPTGAVYSRK
     VLEEIAQVAR ENDLLILADE IYDRILYDGA EHISMAQVAP DMLCITFNGL SKAYRVAGYR
     AGWMILTGPK HHAAGFIEGL ELLASTRLCP NAPAQHAVQV ALGGRQSIYD LTCKGGRLLE
     QRNVAYEKLN EIPGISCTKP MGALYCFPKI DRNVYDIHDD AQFMLDLLRA EKILMVQGTG
     FNWPEPDHFR VVTLPWAKDL EIAIDRIGNF LASYKQ
//