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Database: UniProt
Entry: Q7P0R7_CHRVO
LinkDB: Q7P0R7_CHRVO
Original site: Q7P0R7_CHRVO 
ID   Q7P0R7_CHRVO            Unreviewed;       203 AA.
AC   Q7P0R7;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   OrderedLocusNames=CV_0499 {ECO:0000313|EMBL:AAQ58176.1};
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ58176.1, ECO:0000313|Proteomes:UP000001424};
RN   [1] {ECO:0000313|EMBL:AAQ58176.1, ECO:0000313|Proteomes:UP000001424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA   de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA   de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA   Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA   Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA   Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA   Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA   Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA   Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA   Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA   Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA   Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA   Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC         methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC         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|ARBA:ARBA00010638, ECO:0000256|RuleBase:RU361279}.
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DR   EMBL; AE016825; AAQ58176.1; -; Genomic_DNA.
DR   RefSeq; WP_011134054.1; NC_005085.1.
DR   AlphaFoldDB; Q7P0R7; -.
DR   STRING; 243365.CV_0499; -.
DR   KEGG; cvi:CV_0499; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_0_0_4; -.
DR   OrthoDB; 9801938at2; -.
DR   Proteomes; UP000001424; 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; NagB/RpiA/CoA transferase-like; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02727; MTHFS_bact; 1.
DR   PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   PIRSF; PIRSF006806; FTHF_cligase; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR006806-
KW   1}; Ligase {ECO:0000313|EMBL:AAQ58176.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006806-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001424}.
FT   BINDING         10..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         136..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ   SEQUENCE   203 AA;  22902 MW;  9F712EBB6D9753A2 CRC64;
     MTSTSPDIDK PALRRQLRRA RMALPPACRA AAARAIARHA SRLLKRGKRV GGYLAAGSEL
     DLAEVMNAAL WRGAAVYLPQ IPKRGRRLWF TRLDAADRWY LHPRYRILEY AGARLRAERL
     DVVFVPLLGV DRDGYRMGQG GGFYDSTLAF RRRHALSGKP LLVGVAFDCQ LVDAVPREAW
     DVRLDWLLTE SGLRRLPLRS ARA
//
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