ID A0A0L8GPH4_OCTBM Unreviewed; 167 AA.
AC A0A0L8GPH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|ARBA:ARBA00038966, ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|ARBA:ARBA00038966, ECO:0000256|RuleBase:RU361279};
GN ORFNames=OCBIM_22030122mg {ECO:0000313|EMBL:KOF78923.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF78923.1};
RN [1] {ECO:0000313|EMBL:KOF78923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF78923.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF78923.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
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|ARBA:ARBA00036539,
CC 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; KQ420902; KOF78923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8GPH4; -.
DR EnsemblMetazoa; Ocbimv22030123m; Ocbimv22030123m.p; Ocbimv22030122m.g.
DR EnsemblMetazoa; XM_014923669.1; XP_014779155.1; LOC106875500.
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}; 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}.
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 103..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 167 AA; 18863 MW; 80158DB1296F6D85 CRC64;
MNLPEFEASK RISIYLSTTD EVRTESIMKK ILASNKTCFI PHYSGTSMKM VALKSLEDYE
NLPLTNWNIK QPSDDDIRTD ALETGGLDLI VMPGLAFSLA GARLGRGKGY YDAYLKKCYE
YGNKPITIAL CFHQMLFDNI PVIPGSDMFV NKVIYPDEAD LMESRTR
//