ID   Y2256_MYCBO             Reviewed;         364 AA.
AC   P63501; A0A1R3Y2Q9; Q10503; X2BK63;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Uncharacterized aminotransferase Mb2256c;
DE            EC=2.6.1.-;
GN   OrderedLocusNames=BQ2027_MB2256C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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; LT708304; SIU00864.1; -; Genomic_DNA.
DR   RefSeq; NP_855905.1; NC_002945.3.
DR   RefSeq; WP_003411503.1; NC_002945.4.
DR   AlphaFoldDB; P63501; -.
DR   SMR; P63501; -.
DR   EnsemblBacteria; SIU00864; SIU00864; BQ2027_MB2256C.
DR   PATRIC; fig|233413.5.peg.2473; -.
DR   OMA; RDPWSVN; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..364
FT                   /note="Uncharacterized aminotransferase Mb2256c"
FT                   /id="PRO_0000123928"
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  38937 MW;  1926E58CAA78B2AB CRC64;
     MLWILGPHTG PLLFDAVASL DTSPLAAARY HGDQDVAPGV LDFAVNVRHD RPPEWLVRQL
     AALLPELARY PSTDDVHRAQ DAVAERHGRT RDEVLPLVGA AEGFALLHNL SPVRAAIVVP
     AFTEPAIALS AAGITAHHVV LKPPFVLDTA HVPDDADLVV VGNPTNPTSV LHLREQLLEL
     RRPGRILVVD EAFADWVPGE PQSLADDSLP DVLVLRSLTK TWSLAGLRVG YALGSPDVLA
     RLTVQRAHWP LGTLQLTAIA ACCAPRAVAA AAADAVRLTA LRAEMVAGLR SVGAEVVDGA
     APFVLFNIAD ADGLRNYLQS KGIAVRRGDT FVGLDARYLR AAVRPEWPVL VAAIAEWAKR
     GGRR