(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NV84_YERPA

ID   A0A0E1NV84_YERPA        Unreviewed;       198 AA.
AC   A0A0E1NV84;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   OrderedLocusNames=YPA_0354 {ECO:0000313|EMBL:ABG12322.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12322.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12322.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12322.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-formyltetrahydrofolate + ATP = 5,10-
CC         methenyltetrahydrofolate + ADP + phosphate;
CC         Xref=Rhea:RHEA:10488, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57455, ChEBI:CHEBI:57457, ChEBI:CHEBI:456216;
CC         EC=6.3.3.2; Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000256|RuleBase:RU361279}.
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DR   EMBL; CP000308; ABG12322.1; -; Genomic_DNA.
DR   RefSeq; WP_002209955.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12322; ABG12322; YPA_0354.
DR   EnsemblBacteria; AJJ79173; AJJ79173; CH58_3202.
DR   KEGG; ypa:YPA_0354; -.
DR   PATRIC; fig|360102.15.peg.3361; -.
DR   KO; K01934; -.
DR   OMA; GIVFDFA; -.
DR   BioCyc; YPES360102:GHZU-373-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10420; -; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR23407:SF1; PTHR23407:SF1; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   PIRSF; PIRSF006806; FTHF_cligase; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR02727; MTHFS_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NV84.
DR   SWISS-2DPAGE; A0A0E1NV84.
KW   ATP-binding {ECO:0000256|RuleBase:RU361279};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Ligase {ECO:0000313|EMBL:ABG12322.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361279}.
SQ   SEQUENCE   198 AA;  23114 MW;  916F47DE795CC550 CRC64;
     MPQNPQHALE RQRIRAEIRE HRRLLTPVQQ QQSAHLAAQH IAEHPKIQQA HTVAVFLSFD
     GELDTQPIIE QLWQQKKQVY LPVLHPFSPG NLLFLRYRPE SPLIRNRLKI LEPQLDVREV
     LPLHQLDVVI TPLVAFDRHG QRLGMGGGFY DRTLQRWQQN GPYPIGLAHD CQLVDKLPSE
     YWDVPLPEIV TPAKVWQW
//

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