ID   ARFB_METM7              Reviewed;         221 AA.
AC   A6VHX1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase {ECO:0000255|HAMAP-Rule:MF_02116};
DE            Short=FAPy deformylase {ECO:0000255|HAMAP-Rule:MF_02116};
DE            EC=3.5.1.102 {ECO:0000255|HAMAP-Rule:MF_02116};
DE   AltName: Full=Formamide hydrolase {ECO:0000255|HAMAP-Rule:MF_02116};
GN   Name=arfB {ECO:0000255|HAMAP-Rule:MF_02116}; OrderedLocusNames=MmarC7_0980;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the formamide of 2-amino-5-
CC       formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy)
CC       to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate
CC       (APy). {ECO:0000255|HAMAP-Rule:MF_02116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-
CC         4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one
CC         5'-phosphate + formate + H(+); Xref=Rhea:RHEA:27282,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:57258, ChEBI:CHEBI:59545; EC=3.5.1.102;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02116};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Requires one Fe(2+) ion for activity. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Requires an additional second metal ion that could be Fe(2+) or
CC       Zn(2+). {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02116}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02116}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02116}.
CC   -!- SIMILARITY: Belongs to the creatininase superfamily. FAPy deformylase
CC       family. {ECO:0000255|HAMAP-Rule:MF_02116}.
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DR   EMBL; CP000745; ABR66047.1; -; Genomic_DNA.
DR   RefSeq; WP_011977362.1; NC_009637.1.
DR   AlphaFoldDB; A6VHX1; -.
DR   STRING; 426368.MmarC7_0980; -.
DR   EnsemblBacteria; ABR66047; ABR66047; MmarC7_0980.
DR   GeneID; 5329593; -.
DR   KEGG; mmz:MmarC7_0980; -.
DR   eggNOG; arCOG04536; Archaea.
DR   HOGENOM; CLU_1192640_0_0_2; -.
DR   OMA; FLIINCH; -.
DR   OrthoDB; 84020at2157; -.
DR   UniPathway; UPA00071; -.
DR   UniPathway; UPA00275; -.
DR   GO; GO:0043729; F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10310; -; 1.
DR   HAMAP; MF_02116; FAPy_deform; 1.
DR   InterPro; IPR024087; Creatininase-like_sf.
DR   InterPro; IPR003785; Creatininase/forma_Hydrolase.
DR   InterPro; IPR024901; FAPy_deformylase.
DR   PANTHER; PTHR35005; PTHR35005; 1.
DR   Pfam; PF02633; Creatininase; 1.
DR   SUPFAM; SSF102215; SSF102215; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Zinc.
FT   CHAIN           1..221
FT                   /note="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-
FT                   one 5'-monophosphate deformylase"
FT                   /id="PRO_0000406928"
FT   BINDING         29
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT   BINDING         31
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT   BINDING         40
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT   BINDING         40
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
SQ   SEQUENCE   221 AA;  24649 MW;  81E494BD21967DEC CRC64;
     MVDLRYGSGN IFNEKVHGIG IIALGSFLEN HGSALPIDTD AKIASYIALN VSIITGAKFL
     GVVLPSTEYS YVKHGIHDSI KDVINYIKYL VENGRKIGIN KFLIINCHGG NTLIKDEISK
     LNHENCFIRM ENVCLTHAAT DEVSLGYAVG ILSEDKMKTH DPEIYEEIGM VGLKEAREKN
     EAIDLEARSV EENGVFLDRT HGRFLLNELI NNYVEIVRNM I