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Database: UniProt
Entry: A0A197K0A2_9FUNG
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Original site: A0A197K0A2_9FUNG 
ID   A0A197K0A2_9FUNG        Unreviewed;       310 AA.
AC   A0A197K0A2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-JUL-2019, entry version 16.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_03158};
DE   AltName: Full=Thiazole biosynthetic enzyme {ECO:0000256|HAMAP-Rule:MF_03158};
DE            EC=2.4.2.60 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   ORFNames=K457DRAFT_149073 {ECO:0000313|EMBL:OAQ29919.1};
OS   Mortierella elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota;
OC   Mortierellomycotina; Mortierellomycetes; Mortierellales;
OC   Mortierellaceae; Mortierella.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ29919.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ29919.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ29919.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P.,
RA   Wu S., Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A.,
RA   Zienkiewicz K., Morin E., Tisserant E., Splivallo R., Hainaut M.,
RA   Henrissat B., Ohm R., Kuo A., Yan J., Lipzen A., Nolan M., Labutti K.,
RA   Barry K., Goldstein A., Labbe J., Schadt C., Tuskan G., Grigoriev I.,
RA   Martin F., Vilgalys R., Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis
RT   in the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in biosynthesis of the thiamine precursor
CC       thiazole. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid
CC       (ADT), an adenylated thiazole intermediate. The reaction includes
CC       an iron-dependent sulfide transfer from a conserved cysteine
CC       residue of the protein to a thiazole intermediate. The enzyme can
CC       only undergo a single turnover, which suggests it is a suicide
CC       enzyme. May have additional roles in adaptation to various stress
CC       conditions and in DNA damage tolerance. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) =
CC         [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-
CC         COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151;
CC         EC=2.4.2.60; Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03158};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-200 to a reaction intermediate, generating a dehydroalanine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
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DR   EMBL; KV442038; OAQ29919.1; -; Genomic_DNA.
DR   EnsemblFungi; OAQ29919; OAQ29919; K457DRAFT_149073.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_03158; THI4; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027495; Sti35.
DR   InterPro; IPR002922; Thi4_fam.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00292; TIGR00292; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078512};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03158};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION        1     22       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A197K0A2}.
FT   REGION       97     98       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      279    281       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      77     77       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     105    105       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     171    171       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     202    202       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     217    217       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     269    269       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     200    200       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   310 AA;  32784 MW;  78B7771C043575D1 CRC64;
     MAATNGNHVA SSTATTTSTA QGNGAINLIG EPKYDLNDLH FNPIKEADVS REMTRRYMTD
     MIDHAETDVV VIGAGSAGLS CAWELSKNPD IQVTVIEQSV SPGGGAWLGG QLFSAMIVRK
     PGHHFLAEVG VPFEDCNENY VVVKHAALFT STILSKLLMR PNVKLFNALA AEDLIVKNGR
     VAGVVTNWTL VTLHHDTQSC MDPNVIEAKV VVSSTGHDGP MGASGVKRLQ KIGLIKNVPG
     MIALDMNAAE DGIVANTREV VPGMVITGME VAELDGVPRM GPTFGAMMLS GQKAAHCALK
     SLGLDNVLTN
//
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