ARFB_METTH
ID ARFB_METTH Reviewed; 234 AA.
AC O26747;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MTH_651;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB85156.1; -; Genomic_DNA.
DR PIR; F69186; F69186.
DR AlphaFoldDB; O26747; -.
DR SMR; O26747; -.
DR STRING; 187420.MTH_651; -.
DR EnsemblBacteria; AAB85156; AAB85156; MTH_651.
DR KEGG; mth:MTH_651; -.
DR PATRIC; fig|187420.15.peg.630; -.
DR HOGENOM; CLU_1192640_0_0_2; -.
DR OMA; FLIINCH; -.
DR UniPathway; UPA00071; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000005223; 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..234
FT /note="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-
FT one 5'-monophosphate deformylase"
FT /id="PRO_0000406917"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 32
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 41
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 41
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02116"
SQ SEQUENCE 234 AA; 25717 MW; 7BCCE1736A593450 CRC64;
MLVELNLDAG NIISEDVHRI GILAVGSHLE NHGPALPIDT DAKIASYVAL EAALRTGARF
LGVLYAASEF PYVKHGIHMD RDELVERELK PVLRKARRLL NLEAAVIVNG HGGNKLEDCM
DDLEEELGLE IAWNNRIVEI EGPHAGSGEL SAGLILGIAD LRRLDECIPE LYPEIGMIGL
KEAREANREI DKAARICERD GVNPDPVLGQ RILDDAVESV ISDVKELLKI IQEF
