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FTHS_CERSK
ID   FTHS_CERSK              Reviewed;         557 AA.
AC   B9KLK4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=RSKD131_2019;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC         formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR   EMBL; CP001150; ACM01879.1; -; Genomic_DNA.
DR   RefSeq; WP_015921138.1; NC_011963.1.
DR   AlphaFoldDB; B9KLK4; -.
DR   SMR; B9KLK4; -.
DR   EnsemblBacteria; ACM01879; ACM01879; RSKD131_2019.
DR   GeneID; 67447411; -.
DR   KEGG; rsk:RSKD131_2019; -.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001597; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01268; FTHFS; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT   CHAIN           1..557
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000185261"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   557 AA;  59588 MW;  6C8A3F19157AFEF3 CRC64;
     MAVQTDIEIA RAARKKPIQE IGAGLGIPAE ALIPYGHDKA KVGQGFIRGL EGRPDGKLIL
     VTAINPTPAG EGKTTTTVGL GDGLNRIGKK AVICIREASL GPNFGMKGGA AGGGRAQVVP
     MEDMNLHFTG DFHAITAAHN LLAAMIDNHI YWGNALELDA RRITWRRVMD MNDRALRDTV
     VNLGGVANGF PRQTGFDITV ASEVMAILCL ADDLEDLERR LGRIVVGYRR DKSPVYCRDL
     KAAGAMAVLL KDAMQPNLVQ TIENNPAFVH GGPFANIAHG CNSVIATRTA LKLADYVVTE
     AGFGADLGAE KFFDIKCRLA GLKPSAAVVV ATVRALKMNG GVAREDLGRE DVAALRRGCA
     NLGRHIANVK GFGVPVVVAI NHFTTDTEAE IEAVRAYAAG QGAEAFLCRH WAEGSAGIED
     LAQKVVELAE APSMFAPLYP DDMPLFEKME TVARRIYHAH DVIADHVIRD QLRTWEEAGY
     GALPVCMAKT QYSFTTDAAI RGAPEGHSIP IREVRLAAGA GFVVAICGEI RTMPGLPSQP
     AAELIHLDEE GRIEGLF
 
 
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