ID I4ZRB8_9GAMM Unreviewed; 196 AA.
AC I4ZRB8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN ORFNames=HADU_10662 {ECO:0000313|EMBL:EIM38760.1};
OS Acinetobacter sp. HA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM38760.1, ECO:0000313|Proteomes:UP000018434};
RN [1] {ECO:0000313|EMBL:EIM38760.1, ECO:0000313|Proteomes:UP000018434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:EIM38760.1,
RC ECO:0000313|Proteomes:UP000018434};
RX PubMed=22933775; DOI=10.1128/JB.01194-12;
RA Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT the Polyphagous Insect Pest Helicoverpa armigera.";
RL J. Bacteriol. 194:5156-5156(2012).
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:EIM38760.1}.
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DR EMBL; AJXD01000053; EIM38760.1; -; Genomic_DNA.
DR RefSeq; WP_004810740.1; NZ_AJXD01000053.1.
DR AlphaFoldDB; I4ZRB8; -.
DR PATRIC; fig|1173062.3.peg.2092; -.
DR Proteomes; UP000018434; 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 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}; Ligase {ECO:0000313|EMBL:EIM38760.1};
KW 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 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 137..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 196 AA; 23351 MW; D0D8F234532945DD CRC64;
MYTTVQELRK KIRQARRRIS RFEQKKSAQQ VLNLLRSNPQ FIHSQHVGLY LDAFGEIRTQ
QIIEYCFSIG KKVYLPVICN MNQRLEWVRI NKHLYRNKRF FHHRLGMREP MQSRGLHVSK
LDLLIMPLLI CDYRGTRIGM GGGYYDRTLA TAYKKPYRLG LAHDLQLVET SLPREKWDQP
VDALLTPTRL LHFKRL
//
