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Database: UniProt/SWISS-PROT
Entry: AAT_MYCTO
LinkDB: AAT_MYCTO
Original site: AAT_MYCTO 
ID   AAT_MYCTO               Reviewed;         429 AA.
AC   P9WQ90; L0T6D2; O33267; P63498;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   05-DEC-2018, entry version 25.
DE   RecName: Full=Probable aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=MT0351;
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.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate +
CC         oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991;
CC         EC=2.6.1.1;
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}.
DR   EMBL; AE000516; AAK44574.1; -; Genomic_DNA.
DR   PIR; H70506; H70506.
DR   RefSeq; WP_003401733.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WQ90; -.
DR   SMR; P9WQ90; -.
DR   EnsemblBacteria; AAK44574; AAK44574; MT0351.
DR   KEGG; mtc:MT0351; -.
DR   PATRIC; fig|83331.31.peg.372; -.
DR   KO; K14260; -.
DR   OrthoDB; POG091H05QF; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN         1    429       Probable aspartate aminotransferase.
FT                                /FTId=PRO_0000426817.
FT   MOD_RES     265    265       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   429 AA;  47350 MW;  7B4944351190071A CRC64;
     MDNDGTIVDV TTHQLPWHTA SHQRQRAFAQ SAKLQDVLYE IRGPVHQHAA RLEAEGHRIL
     KLNIGNPAPF GFEAPDVIMR DIIQALPYAQ GYSDSQGILS ARRAVVTRYE LVPGFPRFDV
     DDVYLGNGVS ELITMTLQAL LDNGDQVLIP SPDYPLWTAS TSLAGGTPVH YLCDETQGWQ
     PDIADLESKI TERTKALVVI NPNNPTGAVY SCEILTQMVD LARKHQLLLL ADEIYDKILY
     DDAKHISLAS IAPDMLCLTF NGLSKAYRVA GYRAGWLAIT GPKEHASSFI EGIGLLANMR
     LCPNVPAQHA IQVALGGHQS IEDLVLPGGR LLEQRDIAWT KLNEIPGVSC VKPAGALYAF
     PRLDPEVYDI DDDEQLVLDL LLSEKILVTQ GTGFNWPAPD HLRLVTLPWS RDLAAAIERL
     GNFLVSYRQ
//
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