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Protein

High-potential iron-sulfur protein

Gene

hip

Organism
Rhodocyclus tenuis (Rhodospirillum tenue)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria.

Redox potential

E0 is +330 mV.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi25 – 251Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi40 – 401Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi55 – 551Iron-sulfur (4Fe-4S)1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
High-potential iron-sulfur protein
Short name:
HiPIP
Gene namesi
Name:hip
OrganismiRhodocyclus tenuis (Rhodospirillum tenue)
Taxonomic identifieri1066 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeRhodocyclus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262High-potential iron-sulfur proteinPRO_0000220428Add
BLAST

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

Secondary structure

1
62
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Beta strandi13 – 153Combined sources
Helixi22 – 243Combined sources
Beta strandi38 – 403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISUX-ray1.50A/B1-62[»]
ProteinModelPortaliP33678.
SMRiP33678. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33678.

Family & Domainsi

Sequence similaritiesi

Belongs to the high-potential iron-sulfur protein (HiPIP) family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di4.10.490.10. 1 hit.
InterProiIPR000170. High_potential_FeS_prot.
[Graphical view]
PfamiPF01355. HIPIP. 1 hit.
[Graphical view]
SUPFAMiSSF57652. SSF57652. 1 hit.
PROSITEiPS51373. HIPIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33678-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GTNAAMRKAF NYQDTAKNGK KCSGCAQFVP GASPTAAGGC KVIPGDNQIA
60
PGGYCDAFIV KK
Length:62
Mass (Da):6,296
Last modified:February 1, 1994 - v1
Checksum:i76360061AB43F88D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Missing AA sequence (PubMed:4004266).Curated
Sequence conflicti34 – 341P → A AA sequence (PubMed:4004266).Curated

Sequence databases

PIRiA55789.

Cross-referencesi

Sequence databases

PIRiA55789.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISUX-ray1.50A/B1-62[»]
ProteinModelPortaliP33678.
SMRiP33678. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP33678.

Family and domain databases

Gene3Di4.10.490.10. 1 hit.
InterProiIPR000170. High_potential_FeS_prot.
[Graphical view]
PfamiPF01355. HIPIP. 1 hit.
[Graphical view]
SUPFAMiSSF57652. SSF57652. 1 hit.
PROSITEiPS51373. HIPIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIP2_RHOTE
AccessioniPrimary (citable) accession number: P33678
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 20, 2016
This is version 77 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

3D-structure, Direct protein sequencing

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.