ID   Y2231_MYCTO             Reviewed;         364 AA.
AC   P9WQ88; L0T904; P63500; Q10503;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Uncharacterized aminotransferase MT2290;
DE            EC=2.6.1.-;
GN   OrderedLocusNames=MT2290;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46574.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70777; C70777.
DR   RefSeq; WP_003411503.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ88; -.
DR   SMR; P9WQ88; -.
DR   EnsemblBacteria; AAK46574; AAK46574; MT2290.
DR   KEGG; mtc:MT2290; -.
DR   PATRIC; fig|83331.31.peg.2465; -.
DR   HOGENOM; CLU_017584_3_2_11; -.
DR   Proteomes; UP000001020; 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 MT2290"
FT                   /id="PRO_0000426818"
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