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FTHS1_STRP6
ID   FTHS1_STRP6             Reviewed;         556 AA.
AC   Q5XC12; P82572;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Formate--tetrahydrofolate ligase 1;
DE            EC=6.3.4.3;
DE   AltName: Full=Formyltetrahydrofolate synthetase 1;
DE            Short=FHS 1;
DE            Short=FTHFS 1;
GN   Name=fhs1; Synonyms=fhs, fthS; OrderedLocusNames=M6_Spy0916;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 3-20; 22-33; 54-87; 176-190; 321-331 AND 436-459, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6;
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- MASS SPECTROMETRY: Mass=59531.12; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000003; AAT87051.1; -; Genomic_DNA.
DR   RefSeq; WP_002989724.1; NC_006086.1.
DR   AlphaFoldDB; Q5XC12; -.
DR   SMR; Q5XC12; -.
DR   EnsemblBacteria; AAT87051; AAT87051; M6_Spy0916.
DR   KEGG; spa:M6_Spy0916; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001167; Chromosome.
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   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW   One-carbon metabolism.
FT   CHAIN           1..556
FT                   /note="Formate--tetrahydrofolate ligase 1"
FT                   /id="PRO_0000199397"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   556 AA;  59531 MW;  90C6D132DF20EE3C CRC64;
     MKSDIEIAQS VALQPITDIV KKVGIDGDDI ELYGKYKAKL SFEKMKAVEA NEPGKLILVT
     AINPTPAGEG KSTMSIGLAD ALNQMGKKTM LALREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTANNAL SALIDNHLQQ GNDLGIDPRR IIWKRVLDLN DRALRQVIVG
     LGSPVNGVPR EDGFDITVAS EIMAILCLAT DLKDLKKRLA DIVVAYTYDR KPVYVRDLKV
     EGALTLILKD AIKPNLVQTI YGTPALIHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
     FGADLGAEKF LNIKVPNLPK APDAIVIVAT LRALKMHGGV AKSDLAAENC EAVRLGFANL
     KRHVENMRQF KVPVVVAINE FVADTEAEIA TLKALCEEIK VPVELASVWA NGAEGGLALA
     KTVVRVIDQE AADYKRLYSD EDTLEEKVIN IVTQIYGGKA VQFGPKAKTQ LKQFAEFGWD
     KLPVCMAKTQ YSFSDNPSLL GAPTDFDITI REFVPKTGAG FIVGLTGDVM TMPGLPKVPA
     AMAMDVAENG TALGLF
 
 
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