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Database: UniProt
Entry: A0A1Y5HQ90_9RHOB
LinkDB: A0A1Y5HQ90_9RHOB
Original site: A0A1Y5HQ90_9RHOB 
ID   A0A1Y5HQ90_9RHOB        Unreviewed;       187 AA.
AC   A0A1Y5HQ90;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=A9Q94_07305 {ECO:0000313|EMBL:OUS36995.1};
OS   Rhodobacterales bacterium 56_14_T64.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=1856299 {ECO:0000313|EMBL:OUS36995.1, ECO:0000313|Proteomes:UP000195630};
RN   [1] {ECO:0000313|Proteomes:UP000195630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA   Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT   "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT   within a complex community of hydrocarbon-degraders.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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:OUS36995.1}.
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DR   EMBL; MAAY01000039; OUS36995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5HQ90; -.
DR   Proteomes; UP000195630; 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:OUS36995.1};
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}.
SQ   SEQUENCE   187 AA;  20206 MW;  58175E53F3B46A21 CRC64;
     MTDLTAIKAQ ARKAGFARRK EAHGMHKPGV AGHLSEVLAG YRGVPLSGYM PIRTEIDPVA
     AMAEAAAHGP VGVPVIMSAG QPLKFSRWQP EAPLRDGPFG AKVPEVDDFF DPEILIVPLV
     AFDAQGGRLG YGGGFYDRTL EGLRAKRPTL AIGFAFDAQE AQDLPLEPTD QPLDMLITES
     RVLQFQR
//
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