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Protein

Hydroxylamine reductase

Gene

hcp

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi3 – 31Iron-sulfur (4Fe-4S)6 Publications
Metal bindingi6 – 61Iron-sulfur (4Fe-4S)6 Publications
Metal bindingi15 – 151Iron-sulfur (4Fe-4S)6 Publications
Metal bindingi21 – 211Iron-sulfur (4Fe-4S)6 Publications
Metal bindingi71 – 711Iron-sulfur (4Fe-4S)6 Publications
Metal bindingi244 – 2441Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen5 Publications
Metal bindingi268 – 2681Iron-oxo-sulfur (4Fe-2O-2S)5 Publications
Metal bindingi312 – 3121Iron-oxo-sulfur (4Fe-2O-2S)5 Publications
Metal bindingi406 – 4061Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group5 Publications
Metal bindingi434 – 4341Iron-oxo-sulfur (4Fe-2O-2S)5 Publications
Metal bindingi459 – 4591Iron-oxo-sulfur (4Fe-2O-2S)5 Publications
Metal bindingi494 – 4941Iron-oxo-sulfur (4Fe-2O-2S)5 Publications
Metal bindingi496 – 4961Iron-oxo-sulfur (4Fe-2O-2S)5 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2057-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:DVU_2013
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Hydroxylamine reductasePRO_0000151667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei406 – 4061Cysteine persulfide1 Publication

Proteomic databases

PaxDbiP31101.

Interactioni

Subunit structurei

Monomer.4 Publications

Protein-protein interaction databases

STRINGi882.DVU2013.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Beta strandi15 – 184Combined sources
Helixi25 – 5026Combined sources
Helixi59 – 6810Combined sources
Turni71 – 733Combined sources
Helixi77 – 10630Combined sources
Helixi116 – 1183Combined sources
Helixi124 – 1263Combined sources
Helixi127 – 1315Combined sources
Helixi136 – 1383Combined sources
Helixi142 – 16726Combined sources
Helixi173 – 18513Combined sources
Helixi192 – 22130Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi238 – 2447Combined sources
Helixi246 – 25611Combined sources
Turni257 – 2604Combined sources
Beta strandi262 – 2654Combined sources
Helixi267 – 2748Combined sources
Helixi276 – 2794Combined sources
Beta strandi284 – 2874Combined sources
Helixi292 – 2943Combined sources
Helixi295 – 3028Combined sources
Beta strandi306 – 3116Combined sources
Helixi323 – 3253Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi337 – 3404Combined sources
Helixi352 – 3587Combined sources
Beta strandi370 – 3745Combined sources
Helixi378 – 3836Combined sources
Helixi385 – 3939Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4024Combined sources
Helixi411 – 4133Combined sources
Helixi414 – 4229Combined sources
Beta strandi427 – 4315Combined sources
Helixi434 – 4385Combined sources
Turni439 – 4413Combined sources
Beta strandi450 – 4556Combined sources
Helixi459 – 4613Combined sources
Helixi462 – 47514Combined sources
Helixi481 – 4833Combined sources
Beta strandi484 – 4918Combined sources
Helixi495 – 50612Combined sources
Beta strandi513 – 5175Combined sources
Helixi524 – 53411Combined sources
Helixi542 – 5509Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31101.

Family & Domainsi

Sequence similaritiesi

Belongs to the HCP family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EJ7. Bacteria.
COG1151. LUCA.
KOiK05601.
OMAiAYMKHAN.
OrthoDBiEOG69WFJT.
PhylomeDBiP31101.

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.

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
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. Positions 1-553.
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.
OrthoDBiEOG69WFJT.
PhylomeDBiP31101.

Enzyme and pathway databases

BioCyciDVUL882:GJIL-2057-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP31101.

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

« Hide 'large scale' publications
  1. "The primary structure of a protein containing a putative [6Fe-6S] prismane cluster from Desulfovibrio vulgaris (Hildenborough)."
    Stokkermans J.P.W.G., Pierik A.J., Wolbert R.B.G., Hagen W.R., van Dongen W.M.A.M., Veeger C.
    Eur. J. Biochem. 208:435-442(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. van Dongen W.M.A.M.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 202-204.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  4. "Purification and biochemical characterization of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough)."
    Pierik A.J., Wolbert R.B.G., Mutsaers P.H.A., Hagen W.R., Veeger C.
    Eur. J. Biochem. 206:697-704(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-14, SUBCELLULAR LOCATION, COFACTOR, SUBUNIT.
  5. "Multi-frequency EPR and high-resolution Mossbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein."
    Pierik A.J., Hagen W.R., Dunham W.R., Sands R.H.
    Eur. J. Biochem. 206:705-719(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  6. "The prismane protein resolved -- Mossbauer investigation of a 4Fe cluster with an unusual mixture of bridging ligands and metal coordinations."
    Kroeckel M., Trautwein A.X., Arendsen A.F., Hagen W.R.
    Eur. J. Biochem. 251:454-461(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  7. "The 'prismane' protein resolved: X-ray structure at 1.7-A and multiple spectroscopy of two novel 4Fe clusters."
    Arendsen A.F., Hadden J., Card G., McAlpine A.S., Bailey S., Zaitsev V., Duke E.H.M., Lindley P.F., Kroeckel M., Trautwein A.X., Feiters M.C., Charnock J.M., Garner C.D., Marritt S.J., Thomson A.J., Kooter I.M., Johnson M.K., van den Berg W.A.M., van Dongen W.M.A.M., Hagen W.R.
    J. Biol. Inorg. Chem. 3:81-95(1998)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  8. "Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 A resolution."
    Cooper S.J., Garner C.D., Hagen W.R., Lindley P.F., Bailey S.
    Biochemistry 39:15044-15054(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR.
  9. "Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation."
    Macedo S., Mitchell E.P., Romao C.V., Cooper S.J., Coelho R., Liu M.Y., Xavier A.V., LeGall J., Bailey S., Garner C.D., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
    J. Biol. Inorg. Chem. 7:514-525(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SULFHYDRATION AT CYS-406, SUBUNIT.
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  10. "Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation."
    Aragao D., Macedo S., Mitchell E.P., Romao C.V., Liu M.Y., Frazao C., Saraiva L.M., Xavier A.V., LeGall J., van Dongen W.M.A.M., Hagen W.R., Teixeira M., Carrondo M.A., Lindley P.
    J. Biol. Inorg. Chem. 8:540-548(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  11. "Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 A resolution."
    Aragao D., Mitchell E.P., Frazao C.F., Carrondo M.A., Lindley P.F.
    Acta Crystallogr. D 64:665-674(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR, SUBUNIT.
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  12. "Ferricyanide soaked hybrid cluster protein at 1.2A and xenon mapping of the hydrophobic cavity at 1.8A."
    Cooper S.J., Garner C.D., Hagen W.R., Lindley P.F., Bailey S.
    Submitted (OCT-2000) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER AND IRON-SULFUR-OXYGEN CLUSTER, COFACTOR.

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: December 9, 2015
This is version 129 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.