ARFB_METRM
ID ARFB_METRM Reviewed; 234 AA.
AC D3E3M2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=mru_1283;
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1;
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC47133.1; -; Genomic_DNA.
DR RefSeq; WP_012956082.1; NC_013790.1.
DR AlphaFoldDB; D3E3M2; -.
DR STRING; 634498.mru_1283; -.
DR EnsemblBacteria; ADC47133; ADC47133; mru_1283.
DR GeneID; 8770934; -.
DR KEGG; mru:mru_1283; -.
DR PATRIC; fig|634498.28.peg.1286; -.
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; UP000008680; 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_0000406918"
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 234 AA; 25457 MW; 86D2559AF142AED3 CRC64;
MVELRVNAGN VKNPNVHKIG IIALGSHLEN HGPALPIDTD AKIASHIAFQ ASLESGAKFL
GVIYPAHELK EINHGIHVSL EDLTDEIVKV LKSAKKFLRI SSVIIVNGHG GNLPIVTTLY
DIEERTGLLI TLNSKIIESE GPHGGSGELS MAKALGIIDE SQVENQTNLE EYGEVGLYMF
GEARRNDPNI EEGALDVEEN GVYVDDVYGQ ELLKLAINSV LLDVEKQLDS HYGY
