ID A4HMV1_LEIBR Unreviewed; 456 AA.
AC A4HMV1;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:CAM43492.1};
GN ORFNames=LBRM_34_2750 {ECO:0000313|EMBL:CAM43492.1};
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:CAM43492.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM43492.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43492.1,
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:CAM43492.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43492.1,
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 ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; FR799009; CAM43492.1; -; Genomic_DNA.
DR RefSeq; XP_001568381.1; XM_001568331.1.
DR AlphaFoldDB; A4HMV1; -.
DR STRING; 5660.A4HMV1; -.
DR GeneID; 5419335; -.
DR KEGG; lbz:LBRM_34_2750; -.
DR VEuPathDB; TriTrypDB:LbrM.34.2750; -.
DR VEuPathDB; TriTrypDB:LBRM2903_340036000; -.
DR InParanoid; A4HMV1; -.
DR OMA; IIYGQSE; -.
DR Proteomes; UP000007258; Chromosome 35.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAM43492.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW Transferase {ECO:0000313|EMBL:CAM43492.1}.
FT DOMAIN 25..128
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 153..440
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 456 AA; 48650 MW; CB69543F425649C1 CRC64;
MCNAPGPPLK KRKPQPLPQT EPLPIYLDYN ATTPLCEEAW QEICRIHGTW GNPSSAHPYG
LAAKYELEKA RKKVQVALNA LSSESIIFTS GGTESNNLAI TGGTLALRQR EPRRRYVVSS
NVEHPAVAEV LRYMDGSNPA TSGTASTTDG AKTVSQATVK VVHVAVNPQT GRLDASSLRK
VLNGLPGGPT CVALVSVMFA NNEIGAVNDI KELCRLTKEL CGAACLFHTD AAQSLGKVPV
DVQDTNVDFL SVCGHKFYGP KGVGALYVKP GVAVQNILFG AGHERGIRPG TENVLLAAGI
AEALRFACTN IDRFSAVMRD TRDELLRVLK VELATHDMGL VVNGDVTVAL PNTLNCALFK
RVPNMKTGSP VTYISAQRLI LATGDEVCIS AGSACHSTID EGTEIVVSDP LKAVQVGVDR
AIGTLRISTG RSTTMDDVRR AGKIIARRAA QQFEVE
//
