ARFB_META3
ID ARFB_META3 Reviewed; 242 AA.
AC A6UUS5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, 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=Maeo_0663;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
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; CP000743; ABR56247.1; -; Genomic_DNA.
DR RefSeq; WP_011973379.1; NC_009635.1.
DR AlphaFoldDB; A6UUS5; -.
DR STRING; 419665.Maeo_0663; -.
DR PRIDE; A6UUS5; -.
DR EnsemblBacteria; ABR56247; ABR56247; Maeo_0663.
DR GeneID; 5327096; -.
DR KEGG; mae:Maeo_0663; -.
DR eggNOG; arCOG04536; Archaea.
DR HOGENOM; CLU_1192640_0_0_2; -.
DR OMA; FLIINCH; -.
DR OrthoDB; 84020at2157; -.
DR UniPathway; UPA00071; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000001106; Chromosome.
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; Reference proteome; Zinc.
FT CHAIN 1..242
FT /note="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-
FT one 5'-monophosphate deformylase"
FT /id="PRO_0000406924"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 48
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
SQ SEQUENCE 242 AA; 27090 MW; 261B7B752C1B0230 CRC64;
MEKMENIKNN KINEIKDIEN LRLTSGKIIN KNVHQIGIIA LGSYLENHGT VLPIDTDIKI
ASYIALNVAI QTGAKFLGCV LPSTEYEYVK HGIHNTPNEV VEYIDFLVEQ GKKIGINKFL
IINCHGGNTL INELIEELPY KSDIKLKIKN ITSTHASTEE LSVGYVIGIA DKSKLKEHNP
KDYPEIAMIG LTEARKNNKY IDNEAKIAEK KGITINEDLG NKILKNAINE CILEVELLLN
NK
