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Database: UniProt
Entry: A0A0M8XGL0_9ACTN
LinkDB: A0A0M8XGL0_9ACTN
Original site: A0A0M8XGL0_9ACTN 
ID   A0A0M8XGL0_9ACTN        Unreviewed;       231 AA.
AC   A0A0M8XGL0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=ADK66_24585 {ECO:0000313|EMBL:KOX05822.1};
OS   Micromonospora sp. NRRL B-16802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX05822.1, ECO:0000313|Proteomes:UP000037709};
RN   [1] {ECO:0000313|EMBL:KOX05822.1, ECO:0000313|Proteomes:UP000037709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX05822.1,
RC   ECO:0000313|Proteomes:UP000037709};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOX05822.1}.
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DR   EMBL; LGEB01000086; KOX05822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8XGL0; -.
DR   STRING; 1415541.ADK66_24585; -.
DR   PATRIC; fig|1415541.3.peg.5154; -.
DR   Proteomes; UP000037709; 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:KOX05822.1};
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}.
FT   REGION          207..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24466 MW;  5AF0C27F91A84789 CRC64;
     MRQECCVPEF SDEAEAAREA KRKTRVDLLA RRRTLPGPTR AAAAGRVQAE LVTLVRRLRP
     HRMTAYVPVG SEPGGADLPE VLRAALPADA ELLLPVLRDD LDLDWAAYTG PDALVAAGRG
     IREPVGPRLG VDAVARAELV VVPALAVDLR GRRLGRGGGS YDRALARVPT TALTVVPLHD
     GELVETIPAE AHDLPVRAVV TPADGVRTLD DGPGRAHGVA PHTSAGRTRG E
//
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