ID   Q4FX34_LEIMA            Unreviewed;       412 AA.
AC   Q4FX34; E9AEQ7; Q18L72;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:CAJ40954.1, ECO:0000313|EMBL:CBZ12710.1};
DE            EC=2.6.1.1 {ECO:0000313|EMBL:CAJ40954.1, ECO:0000313|EMBL:CBZ12710.1};
GN   Name=asat {ECO:0000313|EMBL:CAJ40954.1};
GN   ORFNames=LMJF_35_0820 {ECO:0000313|EMBL:CBZ12710.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ40954.1};
RN   [1] {ECO:0000313|EMBL:CBZ12710.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Friedlin {ECO:0000313|EMBL:CBZ12710.1}, and MHOM/IL/81/Friedlin
RC   {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CAJ40954.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MHOM/SU/1973/5-ASKH {ECO:0000313|EMBL:CAJ40954.1};
RX   PubMed=16725143; DOI=10.1016/j.ijpara.2006.03.006;
RA   Mauricio I.L., Yeo M., Baghaei M., Doto D., Pratlong F., Zemanova E.,
RA   Dedet J.P., Lukes J., Miles M.A.;
RT   "Towards multilocus sequence typing of the Leishmania donovani complex:
RT   resolving genotypes and haplotypes for five polymorphic metabolic enzymes
RT   (ASAT, GPI, NH1, NH2, PGD).";
RL   Int. J. Parasitol. 36:757-769(2006).
RN   [3] {ECO:0000313|EMBL:CBZ12710.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Friedlin {ECO:0000313|EMBL:CBZ12710.1}, and MHOM/IL/81/Friedlin
RC   {ECO:0000313|Proteomes:UP000000542};
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).
RN   [4] {ECO:0000313|EMBL:CBZ12710.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Friedlin {ECO:0000313|EMBL:CBZ12710.1};
RA   Aslett M.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0007829|PDB:4H51}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX   PubMed=25945710; DOI=10.1107/S2053230X15001831;
RA   Abendroth J., Choi R., Wall A., Clifton M.C., Lukacs C.M., Staker B.L.,
RA   Van Voorhis W., Myler P., Lorimer D.D., Edwards T.E.;
RT   "Structures of aspartate aminotransferases from Trypanosoma brucei,
RT   Leishmania major and Giardia lamblia.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 71:566-571(2015).
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}.
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; AM117189; CAJ40954.1; -; Genomic_DNA.
DR   EMBL; FR796431; CBZ12710.1; -; Genomic_DNA.
DR   RefSeq; XP_003722477.1; XM_003722429.1.
DR   PDB; 4H51; X-ray; 1.85 A; A/B=1-412.
DR   PDBsum; 4H51; -.
DR   AlphaFoldDB; Q4FX34; -.
DR   SMR; Q4FX34; -.
DR   STRING; 5664.Q4FX34; -.
DR   EnsemblProtists; CBZ12710; CBZ12710; LMJF_35_0820.
DR   GeneID; 12982266; -.
DR   KEGG; lma:LMJF_35_0820; -.
DR   VEuPathDB; TriTrypDB:LmjF.35.0820; -.
DR   VEuPathDB; TriTrypDB:LMJFC_350013900; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_350013800; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_350013300; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; Q4FX34; -.
DR   OMA; PTWPIHE; -.
DR   BRENDA; 2.6.1.1; 2950.
DR   Proteomes; UP000000542; Chromosome 35.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4H51};
KW   Aminotransferase {ECO:0000313|EMBL:CAJ40954.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW   Transferase {ECO:0000313|EMBL:CAJ40954.1}.
FT   DOMAIN          38..402
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   412 AA;  45990 MW;  A6398BDDF00CB5BB CRC64;
     MSTQAAMTTA ERWQKIQAQA PDVIFDLAKR AAAAKGPKAN LVIGAYRDEQ GRPYPLRVVR
     KAEQLLLDMN LDYEYLPISG YQPFIDEAVK IIYGNTVELE NLVAVQTLSG TGAVSLGAKL
     LTRVFDAETT PIYLSDPTWP NHYGVVKAAG WKNICTYAYY DPKTVSLNFE GMKKDILAAP
     DGSVFILHQC AHNPTGVDPS QEQWNEIASL MLAKHHQVFF DSAYQGYASG SLDTDAYAAR
     LFARRGIEVL LAQSFSKNMG LYSERAGTLS LLLKDKTKRA DVKSVMDSLI REEYTCPPAH
     GARLAHLILS NNELRKEWEA ELSAMAERIR TMRRTVYDEL LRLQTPGSWE HVINQIGMFS
     FLGLSKAQCE YCQNHNIFIT VSGRANMAGL THETALMLAQ TINDAVRNVN RE
//