Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B7JGC0

- B7JGC0_BACC0

UniProt

B7JGC0 - B7JGC0_BACC0

Protein

Hydroxylamine reductase

Gene

hcp

Organism
Bacillus cereus (strain AH820)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (10 Feb 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Cofactori

    Binds 1 4Fe-4S cluster.UniRule annotation
    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 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)UniRule 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

    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

    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 annotation (EC:1.7.-.-UniRule annotation)
    Alternative name(s):
    Hybrid-cluster 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

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS 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.
    OMAiFHHHTVL.
    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

    MIGRGWDDMF CYQCEQTPTG GCKVMGVCGK NETIASLQDT IVFGLKGIAA    50
    YRTHAAQLGY TDAFVDATTQ EALYMTLTNS NFNEQEHVDM AMKVGKSALR 100
    VMELLDEAHT NHFGVPEPVQ ITQNRVEGKA IVVTGHNLFA LEELLKQTEG 150
    KEINIYTHSE MLPAHGYPQL KKYKHLKGNI GKAWYDQRRL FEKFTGAILA 200
    TTNCVMPIKG SYSDRFFSYD IAGLEGVQKI ENDNFAPLIQ KALELPEVHM 250
    ESDEQLVTGF HHNTVLSLAP EIIEAVKEGK IKRFFVIAGC DAPGKGGEYY 300
    RELATSLPPE TVILTTSCGK FRFNDVDYGV VPGTEIPRYI DLGQCNNSIS 350
    TVKIAAALAD AFQCEVNELP VSIVLSWFEQ KAVAILLGLF SLGIQDIRIG 400
    PKAPEFISAG VLDVLQETFG LKLITTAAED MEMMLS 436
    Length:436
    Mass (Da):48,154
    Last modified:February 10, 2009 - v1
    Checksum:iA7AE3F1A77454F70
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001283 Genomic DNA. Translation: ACK91399.1.
    RefSeqiYP_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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001283 Genomic DNA. Translation: ACK91399.1 .
    RefSeqi YP_002452408.1. NC_011773.1.

    3D structure databases

    ProteinModelPortali B7JGC0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405535.BCAH820_3458.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACK91399 ; ACK91399 ; BCAH820_3458 .
    GeneIDi 7191337.
    KEGGi bcu:BCAH820_3458.
    PATRICi 18843856. VBIBacCer122868_3437.

    Phylogenomic databases

    eggNOGi COG1151.
    HOGENOMi HOG000007176.
    KOi K05601.
    OMAi FHHHTVL.
    OrthoDBi EOG69WFJT.

    Enzyme and pathway databases

    BioCyci BCER405535:GHSL-3471-MONOMER.

    Family and domain databases

    Gene3Di 1.20.1270.20. 1 hit.
    3.40.50.2030. 2 hits.
    HAMAPi MF_00069. Hydroxylam_reduct.
    InterProi IPR004137. HCP/CODH.
    IPR010048. Hydroxylam_reduct.
    IPR011254. Prismane-like.
    IPR016099. Prismane-like_a/b-sand.
    IPR016100. Prismane_a-bundle.
    [Graphical view ]
    Pfami PF03063. Prismane. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56821. SSF56821. 1 hit.
    TIGRFAMsi TIGR01703. hybrid_clust. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 41 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