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Database: UniProt/TrEMBL
Entry: A4HMB3_LEIBR
LinkDB: A4HMB3_LEIBR
Original site: A4HMB3_LEIBR 
ID   A4HMB3_LEIBR            Unreviewed;       409 AA.
AC   A4HMB3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Putative aspartate aminotransferase {ECO:0000313|EMBL:CAM43298.1};
DE            EC=2.6.1.1 {ECO:0000313|EMBL:CAM43298.1};
GN   ORFNames=LBRM_34_0810 {ECO:0000313|EMBL:CAM43298.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM43298.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM43298.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43298.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM43298.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43298.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; FR799009; CAM43298.1; -; Genomic_DNA.
DR   RefSeq; XP_001568193.1; XM_001568143.1.
DR   AlphaFoldDB; A4HMB3; -.
DR   STRING; 5660.A4HMB3; -.
DR   GeneID; 5419141; -.
DR   KEGG; lbz:LBRM_34_0810; -.
DR   VEuPathDB; TriTrypDB:LbrM.34.0810; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_340013800; -.
DR   InParanoid; A4HMB3; -.
DR   OMA; PTWPIHE; -.
DR   Proteomes; UP000007258; Chromosome 35.
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:0006520; P:amino acid metabolic process; 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; IPR000796; Asp_trans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CAM43298.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW   Transferase {ECO:0000313|EMBL:CAM43298.1}.
FT   DOMAIN          38..400
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   409 AA;  45678 MW;  8417E226C3FEBB18 CRC64;
     MSAQSTMTTA EHWQMIEGQV PDAIFGLAKR AAAAKGPKAN LVIGAYRDDN GIPYPLRVVR
     KAERLLIDMN PDYEYLPISG YQPFIDEAVK MVYGDAVELE NLVAVQSLSG TGALSLGAKL
     LTYVYDAEKT PIYLSNPTWP NHNSIVKGAG WKNIHTYTYY DPKTVSLNFE GMKKDIQAAP
     NGSVFILHQC AHNPTGVDPS QEQWDEIAEL MLAKHHQVFF DSAYQGYASG NLDEDAYAVR
     LFARRGIEVL LAQSFSKNMG LYNERTGTLS LLLKNKTKCA DVKSVLESLI RSEYTCPPAH
     GARLVHLILS NSELRKEWEV ELAAMAERIR TMRRIVYDEL LRLQTPGSWE HVINQIGMFS
     FLGLSKERCQ YCQDHNVFIT LTGRANMAAL THETALLLAQ TINDAVRSG
//
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