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Protein

Hydroxylamine reductase

Gene

hcp

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi3Iron-sulfur (4Fe-4S)6 Publications1
Metal bindingi6Iron-sulfur (4Fe-4S)6 Publications1
Metal bindingi15Iron-sulfur (4Fe-4S)6 Publications1
Metal bindingi21Iron-sulfur (4Fe-4S)6 Publications1
Metal bindingi244Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen5 Publications1
Metal bindingi268Iron-oxo-sulfur (4Fe-2O-2S)5 Publications1
Metal bindingi312Iron-oxo-sulfur (4Fe-2O-2S)5 Publications1
Metal bindingi406Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group5 Publications1
Metal bindingi434Iron-oxo-sulfur (4Fe-2O-2S)5 Publications1
Metal bindingi459Iron-oxo-sulfur (4Fe-2O-2S)5 Publications1
Metal bindingi494Iron-oxo-sulfur (4Fe-2O-2S)5 Publications1
Metal bindingi496Iron-oxo-sulfur (4Fe-2O-2S)5 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:DVU_2013
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001516671 – 553Hydroxylamine reductaseAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei406Cysteine persulfide1 Publication1

Proteomic databases

PaxDbiP31101.

Interactioni

Subunit structurei

Monomer.4 Publications

Protein-protein interaction databases

STRINGi882.DVU2013.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Beta strandi15 – 18Combined sources4
Helixi25 – 50Combined sources26
Helixi59 – 68Combined sources10
Turni71 – 73Combined sources3
Helixi77 – 106Combined sources30
Helixi116 – 118Combined sources3
Helixi124 – 126Combined sources3
Helixi127 – 131Combined sources5
Helixi136 – 138Combined sources3
Helixi142 – 167Combined sources26
Helixi173 – 185Combined sources13
Helixi192 – 221Combined sources30
Beta strandi227 – 230Combined sources4
Beta strandi238 – 244Combined sources7
Helixi246 – 256Combined sources11
Turni257 – 260Combined sources4
Beta strandi262 – 265Combined sources4
Helixi267 – 274Combined sources8
Helixi276 – 279Combined sources4
Beta strandi284 – 287Combined sources4
Helixi292 – 294Combined sources3
Helixi295 – 302Combined sources8
Beta strandi306 – 311Combined sources6
Helixi323 – 325Combined sources3
Beta strandi326 – 329Combined sources4
Beta strandi337 – 340Combined sources4
Helixi352 – 358Combined sources7
Beta strandi370 – 374Combined sources5
Helixi378 – 383Combined sources6
Helixi385 – 393Combined sources9
Beta strandi395 – 397Combined sources3
Beta strandi399 – 402Combined sources4
Helixi411 – 413Combined sources3
Helixi414 – 422Combined sources9
Beta strandi427 – 431Combined sources5
Helixi434 – 438Combined sources5
Turni439 – 441Combined sources3
Beta strandi450 – 455Combined sources6
Helixi459 – 461Combined sources3
Helixi462 – 475Combined sources14
Helixi481 – 483Combined sources3
Beta strandi484 – 491Combined sources8
Helixi495 – 506Combined sources12
Beta strandi513 – 517Combined sources5
Helixi524 – 534Combined sources11
Helixi542 – 550Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E1DX-ray1.72A1-553[»]
1E2UX-ray1.60A1-553[»]
1E9VX-ray1.72A1-553[»]
1GNTX-ray1.25A1-553[»]
1OA1X-ray1.55A1-553[»]
1W9MX-ray1.35A1-553[»]
ProteinModelPortaliP31101.
SMRiP31101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31101.

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
KOiK05601.
OMAiAYMKHAN.
OrthoDBiPOG091H0NWT.
PhylomeDBiP31101.

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.

P31101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFCFQCQETA KNTGCTVKGM CGKPEETANL QDLLIFVLRG IAIYGEKLKE
60 70 80 90 100
LGQPDRSNDD FVLQGLFATI TNANWDDARF EAMISEGLAR RDKLRNAFLA
110 120 130 140 150
VYKAKNGKDF SEPLPEAATW TGDSTAFAEK AKSVGILATE NEDVRSLREL
160 170 180 190 200
LIIGLKGVAA YAEHAAVLGF RKTEIDEFML EALASTTKDL SVDEMVALVM
210 220 230 240 250
KAGGMAVTTM ALLDEANTTT YGNPEITQVN IGVGKNPGIL ISGHDLKDMA
260 270 280 290 300
ELLKQTEGTG VDVYTHGEML PANYYPAFKK YPHFVGNYGG SWWQQNPEFE
310 320 330 340 350
SFNGPILLTT NCLVPLKKEN TYLDRLYTTG VVGYEGAKHI ADRPAGGAKD
360 370 380 390 400
FSALIAQAKK CPPPVEIETG SIVGGFAHHQ VLALADKVVE AVKSGAIKRF
410 420 430 440 450
VVMAGCDGRQ KSRSYYTEVA ENLPKDTVIL TAGCAKYRYN KLNLGDIGGI
460 470 480 490 500
PRVLDAGQCN DSYSLAVIAL KLKEVFGLDD INDLPVSYDI AWYEQKAVAV
510 520 530 540 550
LLALLFLGVK GIRLGPTLPA FLSPNVAKVL VENFNIKPIG TVQDDIAAMM

AGK
Length:553
Mass (Da):59,979
Last modified:December 15, 1998 - v2
Checksum:iDC3FFC3992B51869
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11707 Genomic DNA. Translation: CAA77767.1.
AE017285 Genomic DNA. Translation: AAS96488.1.
PIRiS29861.
RefSeqiWP_010939296.1. NC_002937.3.
YP_011229.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS96488; AAS96488; DVU_2013.
GeneIDi2796735.
KEGGidvu:DVU2013.
PATRICi32063746. VBIDesVul119526_1845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11707 Genomic DNA. Translation: CAA77767.1.
AE017285 Genomic DNA. Translation: AAS96488.1.
PIRiS29861.
RefSeqiWP_010939296.1. NC_002937.3.
YP_011229.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E1DX-ray1.72A1-553[»]
1E2UX-ray1.60A1-553[»]
1E9VX-ray1.72A1-553[»]
1GNTX-ray1.25A1-553[»]
1OA1X-ray1.55A1-553[»]
1W9MX-ray1.35A1-553[»]
ProteinModelPortaliP31101.
SMRiP31101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU2013.

Proteomic databases

PaxDbiP31101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS96488; AAS96488; DVU_2013.
GeneIDi2796735.
KEGGidvu:DVU2013.
PATRICi32063746. VBIDesVul119526_1845.

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
KOiK05601.
OMAiAYMKHAN.
OrthoDBiPOG091H0NWT.
PhylomeDBiP31101.

Miscellaneous databases

EvolutionaryTraceiP31101.

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_DESVH
AccessioniPrimary (citable) accession number: P31101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 132 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.