ARFB_METJA
ID ARFB_METJA Reviewed; 225 AA.
AC Q57580;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase;
DE Short=FAPy deformylase;
DE EC=3.5.1.102;
DE AltName: Full=Formamide hydrolase;
GN Name=arfB; OrderedLocusNames=MJ0116;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, GENE NAME, PH DEPENDENCE,
RP AND SUBUNIT.
RX PubMed=19309161; DOI=10.1021/bi802341p;
RA Grochowski L.L., Xu H., White R.H.;
RT "An iron(II) dependent formamide hydrolase catalyzes the second step in the
RT archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-
RT deazariboflavin.";
RL Biochemistry 48:4181-4188(2009).
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:0000269|PubMed:19309161}.
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:0000269|PubMed:19309161};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19309161};
CC Note=Requires one Fe(2+) ion for activity.
CC {ECO:0000269|PubMed:19309161};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19309161};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19309161};
CC Note=Requires an additional second metal ion that could be Fe(2+) or
CC Zn(2+). {ECO:0000269|PubMed:19309161};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. Has approximately 80% maximal activity at pH 6.5
CC and 40% activity at pH 8.5. {ECO:0000269|PubMed:19309161};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000269|PubMed:19309161}.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC {ECO:0000269|PubMed:19309161}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19309161}.
CC -!- SIMILARITY: Belongs to the creatininase superfamily. FAPy deformylase
CC family. {ECO:0000305}.
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DR EMBL; L77117; AAB98097.1; -; Genomic_DNA.
DR PIR; D64314; D64314.
DR AlphaFoldDB; Q57580; -.
DR SMR; Q57580; -.
DR STRING; 243232.MJ_0116; -.
DR EnsemblBacteria; AAB98097; AAB98097; MJ_0116.
DR KEGG; mja:MJ_0116; -.
DR eggNOG; arCOG04536; Archaea.
DR HOGENOM; CLU_1192640_0_0_2; -.
DR InParanoid; Q57580; -.
DR OMA; FLIINCH; -.
DR PhylomeDB; Q57580; -.
DR BioCyc; MetaCyc:MON-15290; -.
DR BRENDA; 3.5.1.102; 3260.
DR UniPathway; UPA00071; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000000805; 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; IDA:UniProtKB.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0052645; P:F420-0 metabolic process; IDA:UniProtKB.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Hydrolase; Iron; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..225
FT /note="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-
FT one 5'-monophosphate deformylase"
FT /id="PRO_0000106700"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 25305 MW; 929EF2CEC84DE35C CRC64;
MQLRLSSGNV LNEKVHKVGI IALGSFLENH GAVLPIDTDI KIASYIALKA SILTGAKFLG
VVIPSTEYEY VKHGIHNKPE EVYSYMRFLI NEGKKIGVEK FLIVNCHGGN ILVESFLKDL
EYEFDIKVEM INITFTHAST EEVSVGYIIG IAKADEETLK EHNNFEKYPE VGMVGLKEAR
ENNKAIDKEA KVVKRFGVKL DKKLGEKILN NAIEKVVEKI KEMIR
