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Protein

High-potential iron-sulfur protein

Gene

hip

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
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 +360 mV.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi83 – 831Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi100 – 1001Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi114 – 1141Iron-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

Enzyme and pathway databases

BioCyciAVIN572477:GCJK-2319-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
High-potential iron-sulfur protein
Short name:
HiPIP
Gene namesi
Name:hip
Ordered Locus Names:Alvin_2274
OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Taxonomic identifieri572477 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
Proteomesi
  • UP000001441 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 12285High-potential iron-sulfur proteinPRO_0000013438Add
BLAST

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi572477.Alvin_2274.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 546Combined sources
Beta strandi57 – 593Combined sources
Helixi60 – 623Combined sources
Helixi65 – 684Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 773Combined sources
Helixi80 – 823Combined sources
Beta strandi86 – 905Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0YX-ray0.93A38-122[»]
1CKUX-ray1.20A/B38-122[»]
1HIPX-ray2.00A38-122[»]
1HRQNMR-A38-122[»]
1HRRNMR-A38-122[»]
1JS2X-ray1.90A/B/C/D38-122[»]
1NEHNMR-A38-122[»]
1NOENMR-A37-122[»]
ProteinModelPortaliP00260.
SMRiP00260. Positions 38-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00260.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106CXR. Bacteria.
ENOG410Y4MN. LUCA.
HOGENOMiHOG000218005.
OMAiAIPMINL.
OrthoDBiPOG091H048H.

Family and domain databases

Gene3Di4.10.490.10. 1 hit.
InterProiIPR000170. High_potential_FeS_prot.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01355. HIPIP. 1 hit.
[Graphical view]
SUPFAMiSSF57652. SSF57652. 1 hit.
PROSITEiPS51373. HIPIP. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00260-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKPISKSR RDAVKVMLGT AAAIPMINLV GFGTARASAP ANAVAADDAT
60 70 80 90 100
AIALKYNQDA TKSERVAAAR PGLPPEEQHC ANCQFMQADA AGATDEWKGC
110 120
QLFPGKLINV NGWCASWTLK AG
Length:122
Mass (Da):12,762
Last modified:December 15, 1998 - v2
Checksum:iACBBAFC917F32A09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111N → D (PubMed:7451471).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81381 Genomic DNA. Translation: AAB48829.1.
CP001896 Genomic DNA. Translation: ADC63191.1.
RefSeqiWP_012971463.1. NC_013851.1.

Genome annotation databases

EnsemblBacteriaiADC63191; ADC63191; Alvin_2274.
KEGGialv:Alvin_2274.
PATRICi31924328. VBIAllVin64954_2252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81381 Genomic DNA. Translation: AAB48829.1.
CP001896 Genomic DNA. Translation: ADC63191.1.
RefSeqiWP_012971463.1. NC_013851.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0YX-ray0.93A38-122[»]
1CKUX-ray1.20A/B38-122[»]
1HIPX-ray2.00A38-122[»]
1HRQNMR-A38-122[»]
1HRRNMR-A38-122[»]
1JS2X-ray1.90A/B/C/D38-122[»]
1NEHNMR-A38-122[»]
1NOENMR-A37-122[»]
ProteinModelPortaliP00260.
SMRiP00260. Positions 38-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572477.Alvin_2274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADC63191; ADC63191; Alvin_2274.
KEGGialv:Alvin_2274.
PATRICi31924328. VBIAllVin64954_2252.

Phylogenomic databases

eggNOGiENOG4106CXR. Bacteria.
ENOG410Y4MN. LUCA.
HOGENOMiHOG000218005.
OMAiAIPMINL.
OrthoDBiPOG091H048H.

Enzyme and pathway databases

BioCyciAVIN572477:GCJK-2319-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00260.

Family and domain databases

Gene3Di4.10.490.10. 1 hit.
InterProiIPR000170. High_potential_FeS_prot.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01355. HIPIP. 1 hit.
[Graphical view]
SUPFAMiSSF57652. SSF57652. 1 hit.
PROSITEiPS51373. HIPIP. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIP_ALLVD
AccessioniPrimary (citable) accession number: P00260
Secondary accession number(s): D3RMQ3, P96753, Q9R4K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 15, 1998
Last modified: September 7, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.