(data stored in ACNUC7421 zone)

HOGENOM: MECAP1_1_PE1011

ID   MECAP1_1_PE1011                      STANDARD;      PRT;   326 AA.
AC   MECAP1_1_PE1011; Q609Z5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Thiazole synthase; EC=4.-.- -; (MECAP1_1.PE1011).
GN   Name=thiG; OrderedLocusNames=MCA1077;
OS   METHYLOCOCCUS CAPSULATUS STR. BATH.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MECAP1_1.PE1011.
CC       Methylococcus capsulatus str. Bath, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:THIG_METCA
CC   -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-
CC       phosphate (DXP) to produce the thiazole phosphate moiety of
CC       thiamine. Sulfur is provided by the thiocarboxylate moiety of the
CC       carrier protein ThiS. In vitro, sulfur can be provided by H(2)S
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate +
CC       dehydroglycine + [ThiS]-COSH = 4-methyl-5-(2-
CC       phosphonooxyethyl)thiazole + [ThiS]-COOH + CO(2) + 2 H(2)O.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the thiG family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU92650.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000248049 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q609Z5; -.
DR   EMBL; AE017282; AAU92650.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_113552.1; NC_002977.6.
DR   ProteinModelPortal; Q609Z5; -.
DR   SMR; Q609Z5; 14-255.
DR   GeneID; 3103277; -.
DR   GenomeReviews; AE017282_GR; MCA1077.
DR   KEGG; mca:MCA1077; -.
DR   NMPDR; fig|243233.4.peg.121; -.
DR   TIGR; MCA1077; -.
DR   OMA; TAGCFTA; -.
DR   ProtClustDB; PRK11840; -.
DR   BioCyc; MCAP243233:MCA_1077-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00443; ThiG; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR008867; ThiG.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF05690; ThiG; 1.
DR   SUPFAM; SSF110399; ThiG; 1.
DR   HOGENOMDNA; MECAP1_1.PE1011; -.
KW   Complete proteome; Cytoplasm; Lyase; Schiff base;
KW   Thiamine biosynthesis.
SQ   SEQUENCE   326 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRVFVNGEER TVPPGTTLED LIAAMDLAGK RVAVELNLEI VPHGDYGSRV LEPDDRVEIV
     HAIGGGQGDP LVIAGKAYTS RLLVGTGKYK DLAETRAAVE MAGAEIVTVA IRRTNIGQDP
     GQPSLLDVIP PDRYTILPNT AGCYTVEDAV RTCRLARELL GGHRLVKLEV LGDPTTLFPD
     VTATLEAAEI LVRDGFDVMV YTNDDPIIAK RLEEIGCVAV MPLAAPIGSG LGIRNPYNIL
     TIVENAKVPV LVDAGVGTAS DAAVAMELGC DGVLMNTAIA EAKNPVLMAS AMKKAIEAGR
     EAFLAGRMPR RRFASASSPL AGLFFD
//

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