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Entry: A0A2K1II97_PHYPA
LinkDB: A0A2K1II97_PHYPA
Original site: A0A2K1II97_PHYPA 
ID   A0A2K1II97_PHYPA        Unreviewed;       361 AA.
AC   A0A2K1II97;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   03-JUL-2019, entry version 9.
DE   RecName: Full=Thiamine thiazole synthase, chloroplastic {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   Name=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   ORFNames=PHYPA_027693 {ECO:0000313|EMBL:PNR29001.1}, PHYPA_027694
GN   {ECO:0000313|EMBL:PNR29002.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR29001.1, ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:PNR29001.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B.,
RA   Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K.,
RA   Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A.,
RA   Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R.,
RA   Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J.,
RA   Sanderfoot A., Schween G., Shiu S.H., Stueber K., Theodoulou F.L.,
RA   Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L.,
RA   Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R.,
RA   Grigoriev I.V., Quatrano R.S., Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR29001.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D.,
RA   Casacuberta J.M., Vandepoele K., Reski R., Cuming A.C., Tuskan G.A.,
RA   Maumus F., Salse J., Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss
RT   genome structure and evolution.";
RL   Plant J. 93:515-533(2018).
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: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-229 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PNR29001.1}.
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DR   EMBL; ABEU02000023; PNR29001.1; -; Genomic_DNA.
DR   EMBL; ABEU02000023; PNR29002.1; -; Genomic_DNA.
DR   Proteomes; UP000006727; Chromosome 23.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-UniRule.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-UniRule.
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   Chloroplast {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006727};
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   Plastid {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      127    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      308    310       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     107    107       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     135    135       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     200    200       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     231    231       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     246    246       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     298    298       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     229    229       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   361 AA;  38248 MW;  5144B3FC7FF1CEB6 CRC64;
     MAATMSISAA GVATGLGANV ELKSNVGSSS SSVAGVRLFT SRKAQLRRCA APATSASLYS
     DANYDLNNYK FAPIKESIVA REMTRRYMTD MITHADTDVV VVGAGSAGLS CAYELSKNPN
     VKVAIVEQSV SPGGGAWLGG QLFSAMIVRK PAHRFLDEIE VPYEEMENYV VIKHAALFTS
     TIMSKLLARP NVKLFNAVAA EDLIIRGDRV SGVVTNWALV AQNHNTQSCM DPNVMEAKVV
     VSSCGHDGPF GATGVKRLRS IGMIESVPGM KCLDMNAAED AIVKHTREVV PGMIVTGMEV
     AEIDGSPRMG PTFGAMMISG QKAAHLALRA LGLPNEVDGN YKPNVHPELV LASTDDMTAS
     A
//
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