ID E9B405_LEIMU Unreviewed; 795 AA.
AC E9B405;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Thiamine biosynthesis-like protein {ECO:0000313|EMBL:CBZ29972.1};
GN ORFNames=LMXM_32_1680 {ECO:0000313|EMBL:CBZ29972.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29972.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ29972.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29972.1,
RC ECO:0000313|Proteomes:UP000007259};
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 -!- 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; FR799585; CBZ29972.1; -; Genomic_DNA.
DR RefSeq; XP_003878422.1; XM_003878373.1.
DR AlphaFoldDB; E9B405; -.
DR GeneID; 13452027; -.
DR KEGG; lmi:LMXM_32_1680; -.
DR VEuPathDB; TriTrypDB:LmxM.32.1680; -.
DR OMA; NPELYWF; -.
DR OrthoDB; 142238at2759; -.
DR PhylomeDB; E9B405; -.
DR Proteomes; UP000007259; Chromosome 32.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.260.50; -; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.70.1510; THUMP domain-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020536; ThiI_AANH.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF02568; ThiI; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF143437; THUMP domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 224..394
FT /note="Thil AANH"
FT /evidence="ECO:0000259|Pfam:PF02568"
FT DOMAIN 470..546
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 587..779
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 88201 MW; 9DC20939B3D5C247 CRC64;
MPSDRQEEKL PTNPREFPDD RTPNFILKAK NGHFHFMMVE PDVSKNYLWY MSEPKLVRIP
ELEAEMRVTG RRWYATDKAG FELQKRNNAV ATDGEPYVCL HNMKNPELYW FGKRHAEPPV
EQTTLVISVG ELYLKSAIHR KRLVRVLMDN IRRVLQNPQV FRNGDTMIEV RKEIPTKEQL
KLLALLPGIA KIYEASQERE ERKGDPRGAF ICSGAQGIPI TPDQRVLALI SGGIDSPVAA
YRMMTRGCLV NGVHFLNSTN DTASVVEKNR RICERLSTVQ GRFDMHYVDI STLQSQIVAN
VPNHNRTLIY KWFMLSLAAS FDDSCFIVTG DSAGQVASQT VHNISTLYPT ICKAVIAPLI
GVTKNFIIDE ARKINTFDLS IQEGADCCQY MMCKSGANLM MGRRTLEACV RRIKLTELEV
MKEVYRDGKL CESSEFTYYP QSGVRASNNT PPPAGLVQDG SNEDDVHDVV YFDAAAGTKM
AEQVRMAMMR APEGNPNSMH MSGREARMAV EKVRSQLAKV MHVPANDIIF TSGGTESNNI
ALNGYHVVRE PWSHASTSEN PNVPDGATVV KVVDLVNHET GSINRNLIRP EGGRLHIDAS
QALLKIDFGS LDLSEVDSIT VTAHKINGPV GVGAVYLRGL TCNKLFSGGS QEKGIRPGTE
NVPAIVGFGA ALALDRSHSV HKEIDALMTE ELEKMGCEIN RRGETSGYIV HATLPQGYSN
TDVVSRLSTK YHVEIGTGSA CKTNEVNTTV YDTLGKTPAP TRSIRISWDS FATLNDAERV
LSALKNVLGE IKLVR
//
