(data stored in ACNUC7421 zone)

SWISSPROT: A4ATT8_MARSH

ID   A4ATT8_MARSH            Unreviewed;       274 AA.
AC   A4ATT8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Thymidylate synthase {ECO:0000256|HAMAP-Rule:MF_00008};
DE            Short=TS {ECO:0000256|HAMAP-Rule:MF_00008};
DE            Short=TSase {ECO:0000256|HAMAP-Rule:MF_00008};
DE            EC=2.1.1.45 {ECO:0000256|HAMAP-Rule:MF_00008};
GN   Name=thyA {ECO:0000256|HAMAP-Rule:MF_00008};
GN   OrderedLocusNames=FB2170_17276 {ECO:0000313|EMBL:EAR00858.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00858.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00858.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-
CC       5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate
CC       (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as
CC       the methyl donor and reductant in the reaction, yielding
CC       dihydrofolate (DHF) as a by-product. This enzymatic reaction
CC       provides an intracellular de novo source of dTMP, an essential
CC       precursor for DNA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP =
CC         7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00008, ECO:0000256|SAAS:SAAS01115414};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-
CC       type ThyA subfamily. {ECO:0000256|HAMAP-Rule:MF_00008}.
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DR   EMBL; CP002157; EAR00858.1; -; Genomic_DNA.
DR   RefSeq; WP_013304661.1; NC_014472.1.
DR   STRING; 313603.FB2170_17276; -.
DR   EnsemblBacteria; EAR00858; EAR00858; FB2170_17276.
DR   KEGG; fbc:FB2170_17276; -.
DR   eggNOG; ENOG4105C0V; Bacteria.
DR   eggNOG; COG0207; LUCA.
DR   HOGENOM; HOG000257899; -.
DR   KO; K00560; -.
DR   OMA; KQYLDLC; -.
DR   OrthoDB; 1212177at2; -.
DR   BioCyc; MSP313603:G1GNS-231-MONOMER; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR   Gene3D; 3.30.572.10; -; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; SSF55831; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 2.
PE   3: Inferred from homology;
DR   PRODOM; A4ATT8.
DR   SWISS-2DPAGE; A4ATT8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS01077523};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00013237}.
FT   DOMAIN        2    274       Thymidylat_synt. {ECO:0000259|Pfam:
FT                                PF00303}.
FT   NP_BIND     123    124       dUMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   NP_BIND     176    179       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   NP_BIND     217    219       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   ACT_SITE    156    156       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00008}.
FT   BINDING      21     21       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING      51     51       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     179    179       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     187    187       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     273    273       5,10-methylenetetrahydrofolate; via
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00008}.
SQ   SEQUENCE   274 AA;  31350 MW;  09FCD037EA337584 CRC64;
     MKQYHDLLKQ VLKDGCQKGD RTGTGTLSVF GHQMRFDLSE GFPMVTTKKL HLKSIVHELL
     WFLKGETNIA YLQENGVRIW NEWADEKGDL GPVYGHQWRN WNSEEIDQIK EVVHSLKNNP
     NSRRMLVSAW NPSVLPDTSK SFSENVGNGK AALPPCHAFF QFYVADGKLS CQLYQRSADI
     FLGVPFNIAS YALFTMMMAQ VCGYEPGEFI HAFGDAHIYN NHMEQVELQL SREPRPLPKM
     VINPEVKDIF DFKFDDFSLV DYNPHPHIKG VVAV
//

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