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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)DescriptionActionsGraphical viewLength
Metal bindingi7Iron-sulfur (4Fe-4S)3 Publications1
Metal bindingi10Iron-sulfur (4Fe-4S)3 Publications1
Metal bindingi19Iron-sulfur (4Fe-4S)3 Publications1
Metal bindingi25Iron-sulfur (4Fe-4S)3 Publications1
Metal bindingi241Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen3 Publications1
Metal bindingi265Iron-oxo-sulfur (4Fe-2O-2S)3 Publications1
Metal bindingi309Iron-oxo-sulfur (4Fe-2O-2S)3 Publications1
Metal bindingi400Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group2 Publications1
Metal bindingi428Iron-oxo-sulfur (4Fe-2O-2S)3 Publications1
Metal bindingi453Iron-oxo-sulfur (4Fe-2O-2S)3 Publications1
Metal bindingi488Iron-oxo-sulfur (4Fe-2O-2S)2 Publications1
Metal bindingi490Iron-oxo-sulfur (4Fe-2O-2S)2 Publications1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001516662 – 545Hydroxylamine reductaseAdd BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei400Cysteine persulfide; in oxidized form1 Publication1

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi525146.Ddes_1829.

Structurei

Secondary structure

1545
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 16Combined sources3
Beta strandi19 – 22Combined sources4
Helixi29 – 54Combined sources26
Helixi61 – 73Combined sources13
Turni76 – 78Combined sources3
Helixi82 – 101Combined sources20
Helixi111 – 114Combined sources4
Helixi120 – 127Combined sources8
Turni128 – 130Combined sources3
Helixi132 – 134Combined sources3
Helixi138 – 163Combined sources26
Helixi169 – 181Combined sources13
Helixi189 – 218Combined sources30
Beta strandi224 – 227Combined sources4
Beta strandi235 – 241Combined sources7
Helixi243 – 253Combined sources11
Turni254 – 257Combined sources4
Beta strandi259 – 262Combined sources4
Helixi264 – 271Combined sources8
Helixi273 – 277Combined sources5
Beta strandi281 – 284Combined sources4
Beta strandi286 – 288Combined sources3
Helixi289 – 291Combined sources3
Helixi292 – 299Combined sources8
Beta strandi303 – 308Combined sources6
Helixi315 – 318Combined sources4
Beta strandi321 – 324Combined sources4
Beta strandi332 – 335Combined sources4
Beta strandi338 – 340Combined sources3
Helixi346 – 353Combined sources8
Beta strandi364 – 368Combined sources5
Helixi372 – 377Combined sources6
Helixi379 – 387Combined sources9
Beta strandi393 – 396Combined sources4
Helixi405 – 407Combined sources3
Helixi408 – 416Combined sources9
Beta strandi421 – 425Combined sources5
Helixi428 – 432Combined sources5
Turni433 – 435Combined sources3
Beta strandi444 – 449Combined sources6
Helixi453 – 455Combined sources3
Helixi456 – 469Combined sources14
Helixi475 – 477Combined sources3
Beta strandi478 – 485Combined sources8
Helixi489 – 500Combined sources12
Beta strandi507 – 511Combined sources5
Helixi518 – 528Combined sources11
Helixi536 – 542Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

CDDicd01914. HCP. 1 hit.
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]
PANTHERiPTHR30109:SF0. PTHR30109:SF0. 1 hit.
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
PDB 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.
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.

Miscellaneous databases

EvolutionaryTraceiQ01770.

Family and domain databases

CDDicd01914. HCP. 1 hit.
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]
PANTHERiPTHR30109:SF0. PTHR30109:SF0. 1 hit.
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: November 2, 2016
This is version 121 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.