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FTHS_BEII9
ID   FTHS_BEII9              Reviewed;         555 AA.
AC   B2IC30;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=Bind_1654;
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001016; ACB95285.1; -; Genomic_DNA.
DR   RefSeq; WP_012384642.1; NC_010581.1.
DR   AlphaFoldDB; B2IC30; -.
DR   SMR; B2IC30; -.
DR   STRING; 395963.Bind_1654; -.
DR   EnsemblBacteria; ACB95285; ACB95285; Bind_1654.
DR   KEGG; bid:Bind_1654; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001695; 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; PS00722; FTHFS_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..555
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000146675"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  58602 MW;  34F1E34F948057DE CRC64;
     MSSDLEIARA AKLRPIATVA DEAKIPAEAL HSYGLHVAKI DTSLLPKKDR PAKLVLVTAI
     NPTPAGEGKT TTTIGLGDAL RRLGKACVIA LREPSLGPCF GTKGGATGGG YAQIVPMERI
     NLHLTGDFHA ITSAHNLLAA LIDNHLYWGA EPKIDSRKVA WRRVLDMNDR ALRQIVVGLG
     GGGNGYPRET GFDITAASEI MAIFCLSKDL ADLQQRLAQI IVAQDVNKQP VRADALQAVG
     AMTVLLKDAL MPNLVQTLEG TPTFVHGGPF ANIAHGCNSV AATLAAMQLG DYVVTEAGFG
     ADLGAEKFLD IKCRQAGIAP SAAVIVATAR ALKSHGGVAP ADLNKENLDA LKAGLANLGR
     HIANVKKFGL PVVVAINHFL SDTEAEQELI AHTCRDEYGV EAIDCRHWAA GGKGALALAE
     KVIALVEGGT AQFKMLYEDT LPLIEKMRRI AQEIYGAADI SLDAKAKKQL ADIEAQGFGH
     FPVCVAKTQY SFAADPKLLG APTGHIVPIR EVRLSAGAGF VVMICGDIMT MPGLSRQPAA
     WKIGLDAQGN IEGLF
 
 
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