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Protein

Hydroxylamine reductase

Gene

hcp

Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71Iron-sulfur (4Fe-4S)3 Publications
Metal bindingi10 – 101Iron-sulfur (4Fe-4S)3 Publications
Metal bindingi19 – 191Iron-sulfur (4Fe-4S)3 Publications
Metal bindingi25 – 251Iron-sulfur (4Fe-4S)3 Publications
Metal bindingi76 – 761Iron-sulfur (4Fe-4S)3 Publications
Metal bindingi241 – 2411Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen3 Publications
Metal bindingi265 – 2651Iron-oxo-sulfur (4Fe-2O-2S)3 Publications
Metal bindingi309 – 3091Iron-oxo-sulfur (4Fe-2O-2S)3 Publications
Metal bindingi400 – 4001Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group2 Publications
Metal bindingi428 – 4281Iron-oxo-sulfur (4Fe-2O-2S)3 Publications
Metal bindingi453 – 4531Iron-oxo-sulfur (4Fe-2O-2S)3 Publications
Metal bindingi488 – 4881Iron-oxo-sulfur (4Fe-2O-2S)2 Publications
Metal bindingi490 – 4901Iron-oxo-sulfur (4Fe-2O-2S)2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciDDES525146:GIWF-1891-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:Ddes_1829
OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Taxonomic identifieri525146 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002598 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
Initiator methionineiRemoved1 Publication
Chaini2 – 545544Hydroxylamine reductasePRO_0000151666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei400 – 4001Cysteine persulfide; in oxidized form1 Publication

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi525146.Ddes_1829.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Beta strandi19 – 224Combined sources
Helixi29 – 5426Combined sources
Helixi61 – 7313Combined sources
Turni76 – 783Combined sources
Helixi82 – 10120Combined sources
Helixi111 – 1144Combined sources
Helixi120 – 1278Combined sources
Turni128 – 1303Combined sources
Helixi132 – 1343Combined sources
Helixi138 – 16326Combined sources
Helixi169 – 18113Combined sources
Helixi189 – 21830Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi235 – 2417Combined sources
Helixi243 – 25311Combined sources
Turni254 – 2574Combined sources
Beta strandi259 – 2624Combined sources
Helixi264 – 2718Combined sources
Helixi273 – 2775Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi286 – 2883Combined sources
Helixi289 – 2913Combined sources
Helixi292 – 2998Combined sources
Beta strandi303 – 3086Combined sources
Helixi315 – 3184Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi332 – 3354Combined sources
Beta strandi338 – 3403Combined sources
Helixi346 – 3538Combined sources
Beta strandi364 – 3685Combined sources
Helixi372 – 3776Combined sources
Helixi379 – 3879Combined sources
Beta strandi393 – 3964Combined sources
Helixi405 – 4073Combined sources
Helixi408 – 4169Combined sources
Beta strandi421 – 4255Combined sources
Helixi428 – 4325Combined sources
Turni433 – 4353Combined sources
Beta strandi444 – 4496Combined sources
Helixi453 – 4553Combined sources
Helixi456 – 46914Combined sources
Helixi475 – 4773Combined sources
Beta strandi478 – 4858Combined sources
Helixi489 – 50012Combined sources
Beta strandi507 – 5115Combined sources
Helixi518 – 52811Combined sources
Helixi536 – 5427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GN9X-ray2.60A/B2-545[»]
1GNLX-ray1.25A/B2-545[»]
1OA0X-ray1.25A/B2-545[»]
1UPXX-ray1.25A/B2-545[»]
ProteinModelPortaliQ01770.
SMRiQ01770. Positions 2-544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01770.

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000007176.
KOiK05601.
OMAiNSVNELP.
OrthoDBiPOG091H0NWT.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01770-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNAMFCYQC QETVGNKGCT QVGVCGKKPE TAALQDALIY VTKGLGQIAT
60 70 80 90 100
RLRAEGKAVD HRIDRLVTGN LFATITNANF DDDILAERVR MTCAAKKELA
110 120 130 140 150
ASLTDKSGLS DAALWEASEK SAMLAKAGTV GVMATTDDDV RSLRWLITFG
160 170 180 190 200
LKGMAAYAKH ADVLGKHENS LDAFMQEALA KTLDDSLSVA DLVALTLETG
210 220 230 240 250
KFGVSAMALL DAANTGTYGH PEITKVNIGV GSNPGILISG HDLRDLEMLL
260 270 280 290 300
KQTEGTGVDV YTHSEMLPAH YYPAFKKYAH FKGNYGNAWW KQKEEFESFN
310 320 330 340 350
GPVLLTTNCL VPPKDSYKDR VYTTGIVGFT GCKHIPGEIG EHKDFSAIIA
360 370 380 390 400
HAKTCPAPTE IESGEIIGGF AHNQVLALAD KVIDAVKSGA IKKFVVMAGC
410 420 430 440 450
DGRAKSRSYY TDFAEGLPKD TVILTAGCAK YRYNKLNLGD IGGIPRVLDA
460 470 480 490 500
GQCNDSYSLA VIALKLKEVF GLEDVNDLPI VYNIAWYEQK AVIVLLALLS
510 520 530 540
LGVKNIHLGP TLPAFLSPNV AKVLVEQFNI GGITSPQDDL KAFFG
Length:545
Mass (Da):58,659
Last modified:January 23, 2007 - v2
Checksum:iFEFF010FF9FBE4AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11975 Genomic DNA. Translation: CAA78029.1.
CP001358 Genomic DNA. Translation: ACL49726.1.
PIRiS24389.
RefSeqiWP_012625450.1. NC_011883.1.

Genome annotation databases

EnsemblBacteriaiACL49726; ACL49726; Ddes_1829.
KEGGidds:Ddes_1829.
PATRICi21737570. VBIDesDes50650_2120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11975 Genomic DNA. Translation: CAA78029.1.
CP001358 Genomic DNA. Translation: ACL49726.1.
PIRiS24389.
RefSeqiWP_012625450.1. NC_011883.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GN9X-ray2.60A/B2-545[»]
1GNLX-ray1.25A/B2-545[»]
1OA0X-ray1.25A/B2-545[»]
1UPXX-ray1.25A/B2-545[»]
ProteinModelPortaliQ01770.
SMRiQ01770. Positions 2-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi525146.Ddes_1829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL49726; ACL49726; Ddes_1829.
KEGGidds:Ddes_1829.
PATRICi21737570. VBIDesDes50650_2120.

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
HOGENOMiHOG000007176.
KOiK05601.
OMAiNSVNELP.
OrthoDBiPOG091H0NWT.

Enzyme and pathway databases

BioCyciDDES525146:GIWF-1891-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ01770.

Family and domain databases

Gene3Di1.20.1270.20. 2 hits.
3.40.50.2030. 2 hits.
HAMAPiMF_00069. Hydroxylam_reduct. 1 hit.
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...

Entry informationi

Entry nameiHCP_DESDA
AccessioniPrimary (citable) accession number: Q01770
Secondary accession number(s): B8J267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to contain a 6Fe-6S cluster as indicated.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.