(data stored in ACNUC1104 zone)

SWISSPROT: D3VJA4_XENNA

ID   D3VJA4_XENNA            Unreviewed;       663 AA.
AC   D3VJA4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE   AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089};
GN   Name=thiC {ECO:0000256|HAMAP-Rule:MF_00089,
GN   ECO:0000313|EMBL:CBJ88660.1};
GN   OrderedLocusNames=XNC1_0586 {ECO:0000313|EMBL:CBJ88660.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88660.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88660.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC       phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide
CC       (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent
CC       reaction. {ECO:0000256|HAMAP-Rule:MF_00089,
CC       ECO:0000256|SAAS:SAAS00956671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-
CC         adenosyl-L-methionine = 4-amino-2-methyl-5-
CC         (phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate
CC         + 3 H(+) + L-methionine; Xref=Rhea:RHEA:24840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58354,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; EC=4.1.99.17;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00089,
CC         ECO:0000256|SAAS:SAAS01115025};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00089};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine. {ECO:0000256|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00956679}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00089, ECO:0000256|SAAS:SAAS00976596}.
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DR   EMBL; FN667742; CBJ88660.1; -; Genomic_DNA.
DR   RefSeq; WP_013183352.1; NC_014228.1.
DR   STRING; 406817.XNC1_0586; -.
DR   EnsemblBacteria; CBJ88660; CBJ88660; XNC1_0586.
DR   KEGG; xne:XNC1_0586; -.
DR   eggNOG; ENOG4105CBF; Bacteria.
DR   eggNOG; COG0422; LUCA.
DR   HOGENOM; HOG000224484; -.
DR   KO; K03147; -.
DR   OMA; LTWELFR; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.540; -; 1.
DR   HAMAP; MF_00089; ThiC; 1.
DR   InterPro; IPR037509; ThiC.
DR   InterPro; IPR025747; ThiC-associated_dom.
DR   InterPro; IPR038521; ThiC/Bza_sf.
DR   InterPro; IPR002817; ThiC/BzaA/B.
DR   PANTHER; PTHR30557; PTHR30557; 1.
DR   Pfam; PF13667; ThiC-associated; 1.
DR   Pfam; PF01964; ThiC_Rad_SAM; 1.
DR   SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR   TIGRFAMs; TIGR00190; thiC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VJA4.
DR   SWISS-2DPAGE; D3VJA4.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923200};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923199};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923226};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923244};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923246};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923219};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00956670};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923206}.
FT   DOMAIN       53    134       ThiC-associated. {ECO:0000259|Pfam:
FT                                PF13667}.
FT   REGION      379    381       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   REGION      420    423       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   METAL       463    463       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       527    527       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       607    607       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       610    610       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       615    615       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   BINDING     265    265       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     294    294       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     323    323       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     359    359       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     459    459       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     486    486       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
SQ   SEQUENCE   663 AA;  74540 MW;  40F78A0361466698 CRC64;
     MSKSNDTVVS NTAIQNTIIP TADISLQAHP ARPRKAQRDA AQAFINSVQG ITFPNSKRIY
     LEGSRPDIQV PMREIRLSPT LIGSTKENPQ FEENESIPVY DTSGPYGDPT SVLDVQTGLS
     QIRQPWIDER NDTEPVPVLS SDFTQQRLAD AGLDHLRFHH RPHPLKARQG KRVTQLHYAR
     QGIITPEMEF IALRENMGRE RIRSEVLRQQ HPGQNFGANL PENITPEFVR QEVAAGRAII
     PANINHPESE PMIIGRNFLV KVNANIGNSS VTSSIEEEVE KLIWSTRWGA DTVMDLSTGR
     YIHETREWIL RNSPVPIGTV PIYQALEKVN GIAENLTWEM FRDTLLEQAE QGVDYFTIHA
     GVLLRYVPMT AKRLTGIVSR GGSIMAKWCL SHHQENFLYT HFREICEICA AYDVSLSLGD
     GLRPGSIQDA NDEAQFSELH TLGELTKIAW EYDVQVMIEG PGHIPMQLIR RNMTEELEHC
     HEAPFYTLGP LTTDIAPGYD HFTSGIGAAM IGWFGCAMLC YVTPKEHLGL PNKEDVKQGL
     ITYKIAAHAA DLAKGHPGAQ IRDNAMSKAR FEFRWEDQFN LALDPDTARA YHDEALPQES
     GKVAHFCSMC GPKFCSMKIT QDVRDYAAKL EQESGMEQMS ETFRARGSEL YHSADEVAHE
     KYV
//

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