A5UJL1 (ARFB_METS3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
Short name=FAPy deformylase
EC=3.5.1.102

Alternative name(s):
Formamide hydrolase

Gene names

Name:	arfB
Ordered Locus Names:	Msm_0184

Organism

Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]

Taxonomic identifier

420247 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanobrevibacter › Methanobrevibacter smithii

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy) By similarity. HAMAP-Rule MF_02116
Catalytic activity	2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate. HAMAP-Rule MF_02116
Cofactor	Requires one Fe2+ ion for activity By similarity. Requires an additional second metal ion that could be Fe2+ or Zn2+ By similarity.
Pathway	Cofactor biosynthesis; coenzyme F420 biosynthesis. HAMAP-Rule MF_02116 Cofactor biosynthesis; riboflavin biosynthesis. HAMAP-Rule MF_02116
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the creatininase superfamily. FAPy deformylase family.

Ontologies

Keywords
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	F420-0 metabolic process Inferred from electronic annotation. Source: HAMAP riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ferrous iron binding Inferred from electronic annotation. Source: HAMAP hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 230	230	2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase HAMAP-Rule MF_02116		PRO_0000406919
Sites
	Metal binding	29	1	Iron 1 By similarity
	Metal binding	31	1	Iron 2; via tele nitrogen By similarity
	Metal binding	40	1	Iron 1 By similarity
	Metal binding	40	1	Iron 2 By similarity
	Metal binding	109	1	Iron 1; via pros nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5UJL1 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 1DD4AC034C318A07	FASTA	230	25,304
	10 20 30 40 50 60 MAELRYRAGK IKNPRVHKIG VIALGSHLEN HGPALPIDTD AKIGAHIAFQ ASLESGAKFL 70 80 90 100 110 120 GIVFPAYELD EIDHGVHVSL DELKANVIST LNSAKKYLDI EKVVIVNSHG GNIPLMTELY 130 140 150 160 170 180 DIEDKTDLTI IFNNKIISTE GPHGGSGELS MAKVLGIINE AEIENQTDLS KYEEVGLYGF 190 200 210 220 230 KQARENDPNI EEGARDVEEN GVYVDEVYGK QLFDLAINSV VFDIEKLLDF

References

[1]

"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut." Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000678 Genomic DNA. Translation: ABQ86389.1.
RefSeq	YP_001272757.1. NC_009515.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	420247.Msm_0184.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ86389; ABQ86389; Msm_0184.
GeneID	5215758.
KEGG	msi:Msm_0184.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1402.
HOGENOM	HOG000254444.
KO	K14653.
OMA	GMVGLKE.
ProtClustDB	CLSK876077.
Enzyme and pathway databases
BioCyc	MSMI420247:GHWZ-227-MONOMER.
UniPathway	UPA00071. UPA00275.
Family and domain databases
Gene3D	3.40.50.10310. 1 hit.
HAMAP	MF_02116. FAPy_deform.
InterPro	IPR024087. Creatininase-like_dom. IPR003785. Creatininase/forma_Hydrolase. IPR024901. FAPy_deformylase. [Graphical view]
Pfam	PF02633. Creatininase. 1 hit. [Graphical view]
SUPFAM	SSF102215. Creatininase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARFB_METS3

Accession

Primary (citable) accession number: A5UJL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program