ID A0A268TX99_9HELI Unreviewed; 193 AA.
AC A0A268TX99;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BKH43_07135 {ECO:0000313|EMBL:PAF49292.1};
OS Helicobacter sp. 13S00401-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1905758 {ECO:0000313|EMBL:PAF49292.1, ECO:0000313|Proteomes:UP000216091};
RN [1] {ECO:0000313|EMBL:PAF49292.1, ECO:0000313|Proteomes:UP000216091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13S00401-1 {ECO:0000313|EMBL:PAF49292.1,
RC ECO:0000313|Proteomes:UP000216091};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000256|ARBA:ARBA00010638}.
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:PAF49292.1}.
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DR EMBL; MLAR01000015; PAF49292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TX99; -.
DR OrthoDB; 9801938at2; -.
DR Proteomes; UP000216091; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006806-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216091}.
FT BINDING 3..7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 143..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 193 AA; 22668 MW; FC7B79D8B9D71628 CRC64;
MTKELVRKEY KKALLKKSGF NIRDKLAETK ILKLLESKKG LKPRKLKVLL YLNLPHEVSL
YSLIKHLRFN HKDYEVYVPS LISPLISKKT QAKSFKVVKL RLPLKKGHFN IKEPKARVPF
FFKDARMDVL VVPVLGVDKS YKRIGFGKGM YDIFYSLQNP KPYLIFVSRI RNVSRLNVGL
KHDIYSKDYI WSN
//