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Protein

Hydroxylamine reductase

Gene

hcp

Organism
Bacillus cereus (strain AH820)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reduction of hydroxylamine to form NH3 and H2O.UniRule annotationSAAS annotation

Catalytic activityi

NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation
  • hybrid [4Fe-2O-2S] clusterUniRule annotationSAAS annotationNote: Binds 1 hybrid [4Fe-2O-2S] cluster.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi14 – 141Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi22 – 221Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi28 – 281Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi78 – 781Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi136 – 1361Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogenUniRule annotation
Metal bindingi160 – 1601Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi204 – 2041Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi290 – 2901Iron-oxo-sulfur (4Fe-2O-2S); via persulfide groupUniRule annotation
Metal bindingi318 – 3181Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi345 – 3451Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi379 – 3791Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi381 – 3811Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. hydroxylamine reductase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationSAAS annotation

Keywords - Ligandi

4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciBCER405535:GHSL-3471-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxylamine reductaseUniRule annotationSAAS annotation (EC:1.7.99.1UniRule annotationSAAS annotation)
Alternative name(s):
Hybrid-cluster proteinUniRule annotation
Prismane proteinUniRule annotation
Gene namesi
Name:hcpUniRule annotation
Ordered Locus Names:BCAH820_3458Imported
OrganismiBacillus cereus (strain AH820)Imported
Taxonomic identifieri405535 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001363: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei290 – 2901Cysteine persulfideUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi405535.BCAH820_3458.

Structurei

3D structure databases

ProteinModelPortaliB7JGC0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1151.
HOGENOMiHOG000007176.
KOiK05601.
OMAiPEFISPG.
OrthoDBiEOG69WFJT.

Family and domain databases

Gene3Di1.20.1270.20. 1 hit.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct.
InterProiIPR004137. HCP/CODH.
IPR010048. Hydroxylam_reduct.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
IPR016100. Prismane_a-bundle.
[Graphical view]
PfamiPF03063. Prismane. 2 hits.
[Graphical view]
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.

Sequencei

Sequence statusi: Complete.

B7JGC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGRGWDDMF CYQCEQTPTG GCKVMGVCGK NETIASLQDT IVFGLKGIAA
60 70 80 90 100
YRTHAAQLGY TDAFVDATTQ EALYMTLTNS NFNEQEHVDM AMKVGKSALR
110 120 130 140 150
VMELLDEAHT NHFGVPEPVQ ITQNRVEGKA IVVTGHNLFA LEELLKQTEG
160 170 180 190 200
KEINIYTHSE MLPAHGYPQL KKYKHLKGNI GKAWYDQRRL FEKFTGAILA
210 220 230 240 250
TTNCVMPIKG SYSDRFFSYD IAGLEGVQKI ENDNFAPLIQ KALELPEVHM
260 270 280 290 300
ESDEQLVTGF HHNTVLSLAP EIIEAVKEGK IKRFFVIAGC DAPGKGGEYY
310 320 330 340 350
RELATSLPPE TVILTTSCGK FRFNDVDYGV VPGTEIPRYI DLGQCNNSIS
360 370 380 390 400
TVKIAAALAD AFQCEVNELP VSIVLSWFEQ KAVAILLGLF SLGIQDIRIG
410 420 430
PKAPEFISAG VLDVLQETFG LKLITTAAED MEMMLS
Length:436
Mass (Da):48,154
Last modified:February 10, 2009 - v1
Checksum:iA7AE3F1A77454F70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001283 Genomic DNA. Translation: ACK91399.1.
RefSeqiWP_000580247.1. NC_011773.1.
YP_002452408.1. NC_011773.1.

Genome annotation databases

EnsemblBacteriaiACK91399; ACK91399; BCAH820_3458.
GeneIDi7191337.
KEGGibcu:BCAH820_3458.
PATRICi18843856. VBIBacCer122868_3437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001283 Genomic DNA. Translation: ACK91399.1.
RefSeqiWP_000580247.1. NC_011773.1.
YP_002452408.1. NC_011773.1.

3D structure databases

ProteinModelPortaliB7JGC0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405535.BCAH820_3458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK91399; ACK91399; BCAH820_3458.
GeneIDi7191337.
KEGGibcu:BCAH820_3458.
PATRICi18843856. VBIBacCer122868_3437.

Phylogenomic databases

eggNOGiCOG1151.
HOGENOMiHOG000007176.
KOiK05601.
OMAiPEFISPG.
OrthoDBiEOG69WFJT.

Enzyme and pathway databases

BioCyciBCER405535:GHSL-3471-MONOMER.

Family and domain databases

Gene3Di1.20.1270.20. 1 hit.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct.
InterProiIPR004137. HCP/CODH.
IPR010048. Hydroxylam_reduct.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
IPR016100. Prismane_a-bundle.
[Graphical view]
PfamiPF03063. Prismane. 2 hits.
[Graphical view]
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Bacillus cereus AH820."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH820Imported.

Entry informationi

Entry nameiB7JGC0_BACC0
AccessioniPrimary (citable) accession number: B7JGC0
Entry historyi
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: March 4, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.