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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.

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.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the gene encoding the high potential iron-sulfur protein (HiPIP) from the purple sulfur bacterium Chromatium vinosum."
    Bruser T., Truper H.G., Dahl C.
    Biochim. Biophys. Acta 1352:18-22(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome of Allochromatium vinosum DSM 180."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D.
  3. "The complete amino acid sequence of Chromatium high potential iron sulfur protein."
    Dus K., Tedro S., Bartsch R.G.
    J. Biol. Chem. 248:7318-7331(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-122.
  4. "Primary structures of high potential, four-iron-sulfur ferredoxins from the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and Chromatium gracile."
    Tedro S.M., Meyer T.E., Bartsch R.G., Kamen M.D.
    J. Biol. Chem. 256:731-735(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 48; 82 AND 111.
  5. "2-A crystal structure of oxidized Chromatium high potential iron protein."
    Carter C.W. Jr., Kraut J., Freer S.T., Xuong N.H., Alden R.A., Bartsch R.G.
    J. Biol. Chem. 249:4212-4225(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
  6. "Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum."
    Nettesheim D.G., Harder S.R., Feinberg B.A., Otvos J.D.
    Biochemistry 31:1234-1244(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "Sequence-specific assignments of the 1H nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum."
    Gaillard J., Albrand J.-P., Moulis J.-M., Wemmer D.E.
    Biochemistry 31:5632-5639(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  8. "The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR."
    Banci L., Bertini I., Dikiy A., Kastrau D.H.W., Luchinat C., Sompornpisut P.
    Biochemistry 34:206-219(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species."
    Bertini I., Dikiy A., Kastrau D.H., Luchinat C., Sompornpisut P.
    Biochemistry 34:9851-9858(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type protein."
    Bentrop D., Bertini I., Cappozi F., Dikiy A., Eltis L., Luchinat C.
    Biochemistry 35:5928-5936(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANT SER-114.
  11. "Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution."
    Parisini E., Capozzi F., Lubini P., Lamzin V., Luchinat C., Sheldrick G.M.
    Acta Crystallogr. D 55:1773-1784(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS).

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: January 20, 2016
This is version 114 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.