ID   I4BD57_MYCCN            Unreviewed;       443 AA.
AC   I4BD57;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Mycch_0394 {ECO:0000313|EMBL:AFM15214.1};
OS   Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM15214.1, ECO:0000313|Proteomes:UP000006057};
RN   [1] {ECO:0000313|EMBL:AFM15214.1, ECO:0000313|Proteomes:UP000006057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB4 {ECO:0000313|EMBL:AFM15214.1,
RC   ECO:0000313|Proteomes:UP000006057};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL   Submitted (JUN-2012) 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   ---------------------------------------------------------------------------
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; CP003053; AFM15214.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4BD57; -.
DR   STRING; 710421.Mycch_0394; -.
DR   KEGG; mcb:Mycch_0394; -.
DR   PATRIC; fig|710421.3.peg.387; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000006057; 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:AFM15214.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006057};
KW   Transferase {ECO:0000313|EMBL:AFM15214.1}.
FT   DOMAIN          73..433
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   443 AA;  49007 MW;  1A0A2969818F0139 CRC64;
     MPDVGTSGPG KHVDNRGRIV DVSTHQTSWQ AGSSQHSRQR EFTQSSKLQD VLYEIRGPVH
     EHASRLEAEG HRILKLNIGN PAPFGFEAPD VIMRDIIQAL PYAQGYSDSK GIVSARRAVF
     TRYELVEGFP RFDIDDVYLG NGVSELITMT LQALLDNGDQ VLIPAPDYPL WTASTSLAGG
     TPVHYLCDET QGWQPDLADL ESKITDRTKA IVVINPNNPT GAVYGREILT QIADLARKHQ
     LLLLADEIYD KILYDEAEHI AMASVAPDVL TLTFNGLSKA YRVAGYRSGW LVITGPKEHA
     TSFIEGISLL ANMRLCPNVP AQHAIQVALG GHQSIEDLVL PGGRLLEQRD VAWEKLNQIP
     GVSCVKPQGA LYAFPRLDPE VYDVVDDEQL VLDLLLQEKI LVTQGTGFNW PTPDHLRIVT
     LPWARDLANA IERLGNFLVS YRQ
//