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Protein

Formamidase

Gene

amiF

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide. Probably involved in the nitrogen metabolism of H.pylori.1 Publication

Catalytic activityi

Formamide + H2O = formate + NH3.1 Publication

Enzyme regulationi

Inhibited by iodoacetate. Appears to be regulated by the fur protein, but this effect is not mediated at the transcriptional level.2 Publications

pH dependencei

Optimum pH is 6.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei60Proton acceptorBy similarity1
Active sitei133Proton donorBy similarity1
Active sitei166NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.49. 2604.

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidase (EC:3.5.1.49)
Alternative name(s):
Formamide amidohydrolase
Gene namesi
Name:amiF
Ordered Locus Names:HP_1238
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi166C → S or A: Loss of activity. 1 Publication1
Mutagenesisi168D → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002040651 – 334FormamidaseAdd BLAST334

Proteomic databases

PaxDbiO25836.

Expressioni

Inductioni

Unlike the other amidase AmiE, expression of amiF is not repressed by iron.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiO25836. 3 interactors.
MINTiMINT-164907.
STRINGi85962.HP1238.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Helixi29 – 49Combined sources21
Beta strandi53 – 57Combined sources5
Turni60 – 64Combined sources5
Turni68 – 72Combined sources5
Helixi74 – 76Combined sources3
Beta strandi80 – 82Combined sources3
Helixi83 – 95Combined sources13
Beta strandi98 – 105Combined sources8
Beta strandi115 – 121Combined sources7
Beta strandi127 – 132Combined sources6
Turni138 – 140Combined sources3
Helixi156 – 158Combined sources3
Beta strandi160 – 165Combined sources6
Helixi166 – 170Combined sources5
Helixi172 – 180Combined sources9
Beta strandi184 – 192Combined sources9
Beta strandi194 – 196Combined sources3
Helixi197 – 211Combined sources15
Beta strandi214 – 219Combined sources6
Beta strandi221 – 226Combined sources6
Beta strandi232 – 236Combined sources5
Beta strandi242 – 245Combined sources4
Beta strandi253 – 258Combined sources6
Helixi260 – 269Combined sources10
Helixi275 – 278Combined sources4
Turni284 – 288Combined sources5
Helixi297 – 303Combined sources7
Helixi312 – 314Combined sources3
Beta strandi318 – 320Combined sources3
Helixi321 – 323Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DYUX-ray1.75A/B1-334[»]
2DYVX-ray2.00A/B1-334[»]
2E2KX-ray2.50A/B/C/D/E/F1-334[»]
2E2LX-ray2.29A/B/C/D/E/F1-334[»]
ProteinModelPortaliO25836.
SMRiO25836.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO25836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 287CN hydrolaseAdd BLAST274

Sequence similaritiesi

Contains 1 CN hydrolase domain.Curated

Phylogenomic databases

eggNOGiENOG4105DCY. Bacteria.
COG0388. LUCA.
KOiK01455.
OMAiVENNIYQ.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
HAMAPiMF_01243. Formamidase. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR022843. Formamidase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O25836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSIGSMGKP IEGFLVAAIQ FPVPIVNSRK DIDHNIESII RTLHATKAGY
60 70 80 90 100
PGVELIIFPE YSTQGLNTAK WLSEEFLLDV PGKETELYAK ACKEAKVYGV
110 120 130 140 150
FSIMERNPDS NKNPYNTAII IDPQGEIILK YRKLFPWNPI EPWYPGDLGM
160 170 180 190 200
PVCEGPGGSK LAVCICHDGM IPELAREAAY KGCNVYIRIS GYSTQVNDQW
210 220 230 240 250
ILTNRSNAWH NLMYTVSVNL AGYDNVFYYF GEGQICNFDG TTLVQGHRNP
260 270 280 290 300
WEIVTGEIYP KMADNARLSW GLENNIYNLG HRGYVAKPGG EHDAGLTYIK
310 320 330
DLAAGKYKLP WEDHMKIKDG SIYGYPTTGG RFGK
Length:334
Mass (Da):37,291
Last modified:January 1, 1998 - v1
Checksum:iB2845E0902A40420
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08283.1.
PIRiF64674.
RefSeqiNP_208030.1. NC_000915.1.
WP_000534771.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08283; AAD08283; HP_1238.
GeneIDi900367.
KEGGiheo:C694_06390.
hpy:HP1238.
PATRICi20593847. VBIHelPyl33062_1294.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08283.1.
PIRiF64674.
RefSeqiNP_208030.1. NC_000915.1.
WP_000534771.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DYUX-ray1.75A/B1-334[»]
2DYVX-ray2.00A/B1-334[»]
2E2KX-ray2.50A/B/C/D/E/F1-334[»]
2E2LX-ray2.29A/B/C/D/E/F1-334[»]
ProteinModelPortaliO25836.
SMRiO25836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO25836. 3 interactors.
MINTiMINT-164907.
STRINGi85962.HP1238.

Proteomic databases

PaxDbiO25836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD08283; AAD08283; HP_1238.
GeneIDi900367.
KEGGiheo:C694_06390.
hpy:HP1238.
PATRICi20593847. VBIHelPyl33062_1294.

Phylogenomic databases

eggNOGiENOG4105DCY. Bacteria.
COG0388. LUCA.
KOiK01455.
OMAiVENNIYQ.

Enzyme and pathway databases

BRENDAi3.5.1.49. 2604.

Miscellaneous databases

EvolutionaryTraceiO25836.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
HAMAPiMF_01243. Formamidase. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR022843. Formamidase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMIF_HELPY
AccessioniPrimary (citable) accession number: O25836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Asp-168 is probably not involved in the catalytic mechanism, but is probably involved instead in maintenance of the structural integrity of the amidase.1 Publication
Expression of the amiF gene is stimulated in a mutant deficient in arginase activity, suggesting that production of this enzyme is regulated to maintain intracellular nitrogen balance in H.pylori.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.