ARFB_METS3
ID ARFB_METS3 Reviewed; 230 AA.
AC A5UJL1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Msm_0184;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86389.1; -; Genomic_DNA.
DR RefSeq; WP_004034909.1; NC_009515.1.
DR AlphaFoldDB; A5UJL1; -.
DR SMR; A5UJL1; -.
DR STRING; 420247.Msm_0184; -.
DR EnsemblBacteria; ABQ86389; ABQ86389; Msm_0184.
DR GeneID; 5215758; -.
DR KEGG; msi:Msm_0184; -.
DR PATRIC; fig|420247.28.peg.188; -.
DR eggNOG; arCOG04536; Archaea.
DR HOGENOM; CLU_1192640_0_0_2; -.
DR OMA; FLIINCH; -.
DR UniPathway; UPA00071; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000001992; 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; Zinc.
FT CHAIN 1..230
FT /note="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-
FT one 5'-monophosphate deformylase"
FT /id="PRO_0000406919"
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 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
SQ SEQUENCE 230 AA; 25304 MW; 1DD4AC034C318A07 CRC64;
MAELRYRAGK IKNPRVHKIG VIALGSHLEN HGPALPIDTD AKIGAHIAFQ ASLESGAKFL
GIVFPAYELD EIDHGVHVSL DELKANVIST LNSAKKYLDI EKVVIVNSHG GNIPLMTELY
DIEDKTDLTI IFNNKIISTE GPHGGSGELS MAKVLGIINE AEIENQTDLS KYEEVGLYGF
KQARENDPNI EEGARDVEEN GVYVDEVYGK QLFDLAINSV VFDIEKLLDF
