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Database: UniProt
Entry: A0A255ELR7_9ACTN
LinkDB: A0A255ELR7_9ACTN
Original site: A0A255ELR7_9ACTN 
ID   A0A255ELR7_9ACTN        Unreviewed;       217 AA.
AC   A0A255ELR7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=CGZ91_02775 {ECO:0000313|EMBL:OYN92434.1};
OS   Parenemella sanctibonifatiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Parenemella.
OX   NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN92434.1, ECO:0000313|Proteomes:UP000216300};
RN   [1] {ECO:0000313|EMBL:OYN92434.1, ECO:0000313|Proteomes:UP000216300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 150081 {ECO:0000313|EMBL:OYN92434.1,
RC   ECO:0000313|Proteomes:UP000216300};
RA   Bernier A.-M., Bernard K., Domingo M.-C.;
RT   "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYN92434.1}.
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DR   EMBL; NMVJ01000001; OYN92434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255ELR7; -.
DR   OrthoDB; 3242798at2; -.
DR   Proteomes; UP000216300; Unassembled WGS sequence.
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   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361279};
KW   Ligase {ECO:0000313|EMBL:OYN92434.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216300}.
SQ   SEQUENCE   217 AA;  22702 MW;  EE70AF78F06BD433 CRC64;
     MTNHESPVTP GPGPAAKSEL RTVLRARRRG LDRAVVDDRR TAALLRVLAE PPAVVAAYWS
     RPDEPDTHAL IDALVARGVR VLLPCGTDPD WAEHQPGQLR PGTYGVAEPT GTPLGAAALA
     EAGLILCPAL AVDRSGRRLG KGGGWYDRAL LHAAADAELW ALVDVAEVLD QVPTEPHDRP
     VTGWVTEAGL ARAGAPVGLG ARHDLPAPAA PDQAAAR
//
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