Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hydroxylamine reductase

Gene

hcp

Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi8 – 81Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi20 – 201Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi27 – 271Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi77 – 771Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi251 – 2511Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogenUniRule annotation
Metal bindingi275 – 2751Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi319 – 3191Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi407 – 4071Iron-oxo-sulfur (4Fe-2O-2S); via persulfide groupUniRule annotation
Metal bindingi435 – 4351Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi460 – 4601Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi494 – 4941Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation
Metal bindingi496 – 4961Iron-oxo-sulfur (4Fe-2O-2S)UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciSDYS300267:GJEW-2386-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxylamine reductaseUniRule annotation (EC:1.7.99.1UniRule annotation)
Alternative name(s):
Hybrid-cluster proteinUniRule annotation
Short name:
HCPUniRule annotation
Prismane proteinUniRule annotation
Gene namesi
Name:hcpUniRule annotation
Ordered Locus Names:SDY_2390
OrganismiShigella dysenteriae serotype 1 (strain Sd197)
Taxonomic identifieri300267 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000002716 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Hydroxylamine reductasePRO_1000009173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei407 – 4071Cysteine persulfideUniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000007176.
OMAiCAYAQGM.
OrthoDBiEOG69WFJT.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
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. 1 hit.
[Graphical view]
PIRSFiPIRSF000076. HCP. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.

Sequencei

Sequence statusi: Complete.

Q32DZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIMFCVQCEQ TIRTPAGNGC SYAQGMCGKT AETSDLQDLL IAALQGLSAW
60 70 80 90 100
AVKAREYGII NHDVDSFAPR AFFSTLTNVN FDSPRIVGYA REAIALREAL
110 120 130 140 150
KAQCLAVDAN ARVDNPMADL QLVSDDLGEL QRQAAEFTPN KDKAAIGENI
160 170 180 190 200
LGLRLLCLYG LKGAAAYMEH AHVLGQYDND IYAQYHKIMA WLGTWPADMN
210 220 230 240 250
ALLECSMEIG QMNFKVMSIL DAGETGKYGH PTPTQVNVKA TAGKCILISG
260 270 280 290 300
HDLKDLYNLL EQTKGTGVNV YTHGEMLPAH GYPELRKFKH LVGNYGSGWQ
310 320 330 340 350
NQQVEFARFP GPIVMTSNCI IDPTVGAYDD RIWTRSIVGW PGVRHLDGED
360 370 380 390 400
FSAVIAQAQQ MAGFLYSEIP HLITVGFGRQ TLLGAADTLI DLVSREKLRH
410 420 430 440 450
IFLLGGCDGA RGERHYFTDF ATNVPDDCLI LTLACGKYRF NKLEFGDIEG
460 470 480 490 500
LPRLVDAGQC NDAYSAIILA VTLAEKLGCG VNDLPLSLVL SWFEQKAIVI
510 520 530 540 550
LLTLLSLGVK NIVTGPTAPG FLTPDLLAVL NEKFGLRSIT TVEEDMKQLL

SA
Length:552
Mass (Da):60,334
Last modified:December 6, 2005 - v1
Checksum:i308D3ED236A0809E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB62464.1.

Genome annotation databases

EnsemblBacteriaiABB62464; ABB62464; SDY_2390.
PATRICi18694916. VBIShiDys99784_2883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB62464.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB62464; ABB62464; SDY_2390.
PATRICi18694916. VBIShiDys99784_2883.

Phylogenomic databases

HOGENOMiHOG000007176.
OMAiCAYAQGM.
OrthoDBiEOG69WFJT.

Enzyme and pathway databases

BioCyciSDYS300267:GJEW-2386-MONOMER.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
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. 1 hit.
[Graphical view]
PIRSFiPIRSF000076. HCP. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01703. hybrid_clust. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sd197.

Entry informationi

Entry nameiHCP_SHIDS
AccessioniPrimary (citable) accession number: Q32DZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: November 11, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.