ID   ARFB_METM6              Reviewed;         221 AA.
AC   A9A8V8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=MmarC6_0966;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-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; CP000867; ABX01781.1; -; Genomic_DNA.
DR   RefSeq; WP_012193730.1; NC_009975.1.
DR   AlphaFoldDB; A9A8V8; -.
DR   SMR; A9A8V8; -.
DR   STRING; 444158.MmarC6_0966; -.
DR   EnsemblBacteria; ABX01781; ABX01781; MmarC6_0966.
DR   GeneID; 5738476; -.
DR   KEGG; mmx:MmarC6_0966; -.
DR   eggNOG; arCOG04536; Archaea.
DR   HOGENOM; CLU_1192640_0_0_2; -.
DR   OMA; FLIINCH; -.
DR   OrthoDB; 84020at2157; -.
DR   PhylomeDB; A9A8V8; -.
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_0000406927"
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;  24477 MW;  22E47BD0156127DB CRC64;
     MVDLRYGSGN IFDEKVHEIG IIALGSFLEN HGSALPIDTD AKIASYIALN VSIITGAKFL
     GVVIPSTEYS YVKHGIHDSI EDVITYIKYL IENGRKIGIN KFLIVNCHGG NTIILDELSK
     LNFDDCFIQM ESVCLTHAAT EEVSLGYAVG ILSEDKMKTH NPKIYEEIGM VGLKEAREKN
     EAIDLEAKSV EKNGVFLDKT HGKSLLNDLI TNYVEIVRNM I