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Protein

High-potential iron-sulfur protein

Gene

hip

Organism
Thermochromatium tepidum (Chromatium tepidum)
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 +323 mV.

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi46Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi61Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi75Iron-sulfur (4Fe-4S)2 Publications1

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
OrganismiThermochromatium tepidum (Chromatium tepidum)
Taxonomic identifieri1050 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThermochromatium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002204291 – 83High-potential iron-sulfur proteinAdd BLAST83

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

Secondary structure

183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 17Combined sources6
Beta strandi20 – 22Combined sources3
Helixi23 – 25Combined sources3
Helixi28 – 31Combined sources4
Helixi38 – 40Combined sources3
Helixi43 – 45Combined sources3
Beta strandi49 – 55Combined sources7
Beta strandi58 – 61Combined sources4
Beta strandi68 – 70Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EYTX-ray1.50A1-83[»]
1IUAX-ray0.80A1-83[»]
2AMSX-ray1.40A1-83[»]
2FLAX-ray0.95A1-83[»]
3A38X-ray0.70A1-83[»]
3A39X-ray0.72A1-83[»]
5D8VX-ray0.48A1-83[»]
ProteinModelPortaliP80176.
SMRiP80176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80176.

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.

P80176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AAPANAVTAD DPTAIALKYN QDATKSERVA AARPGLPPEE QHCANCQFMQ
60 70 80
ANVGEGDWKG CQLFPGKLIN VNGWCASWTL KAG
Length:83
Mass (Da):8,786
Last modified:October 1, 1993 - v1
Checksum:i92116E4FD2C44E0A
GO

Sequence databases

PIRiS35586.

Cross-referencesi

Sequence databases

PIRiS35586.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EYTX-ray1.50A1-83[»]
1IUAX-ray0.80A1-83[»]
2AMSX-ray1.40A1-83[»]
2FLAX-ray0.95A1-83[»]
3A38X-ray0.70A1-83[»]
3A39X-ray0.72A1-83[»]
5D8VX-ray0.48A1-83[»]
ProteinModelPortaliP80176.
SMRiP80176.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80176.

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 nameiHIP_THETI
AccessioniPrimary (citable) accession number: P80176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 2, 2016
This is version 84 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.