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Protein

Zinc-containing ferredoxin

Gene

zfx

Organism
Acidianus ambivalens (Desulfurolobus ambivalens)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. The 3Fe-4S cluster is reduced by a flavoprotein with NADH oxidase activity from the same organism.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161ZincBy similarity
Metal bindingi19 – 191ZincBy similarity
Metal bindingi34 – 341ZincBy similarity
Metal bindingi45 – 451Iron-sulfur 1 (3Fe-4S)By similarity
Metal bindingi51 – 511Iron-sulfur 1 (3Fe-4S)By similarity
Metal bindingi55 – 551Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi83 – 831Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi89 – 891Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi93 – 931Iron-sulfur 1 (3Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc-containing ferredoxin
Alternative name(s):
Seven-iron ferredoxin
Gene namesi
Name:zfx
OrganismiAcidianus ambivalens (Desulfurolobus ambivalens)
Taxonomic identifieri2283 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeAcidianus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 103103Zinc-containing ferredoxinPRO_0000159173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291N6-methyllysine; partial1 Publication
Modified residuei101 – 1011N6-methyllysine; partial1 Publication

Post-translational modificationi

Lys-29 was found to be 95% monomethylated and Lys-101 was found to be 10% monomethylated.

Keywords - PTMi

Methylation

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Beta strandi12 – 165Combined sources
Beta strandi19 – 235Combined sources
Turni27 – 293Combined sources
Beta strandi36 – 416Combined sources
Turni42 – 443Combined sources
Helixi50 – 545Combined sources
Beta strandi61 – 644Combined sources
Beta strandi72 – 765Combined sources
Helixi80 – 823Combined sources
Helixi88 – 925Combined sources
Beta strandi98 – 1003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VKRX-ray2.01A/B/C/D/E/F/G1-103[»]
ProteinModelPortaliP49949.
SMRiP49949. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49949.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 65294Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini74 – 103304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3636N-terminal extensionAdd
BLAST

Sequence similaritiesi

Contains 2 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR009157. Fd_Zn-bd.
[Graphical view]
PfamiPF13187. Fer4_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000068. Zn_Fdx_Sulfol. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GIDPNYRTSR QVVGEHQGHK VYGPVDPPKV LGIHGTIVGV DFDLCIADGS
60 70 80 90 100
CITACPVNVF QWYDTPGHPA SEKKADPINE QACIFCMACV NVCPVAAIDV

KPP
Length:103
Mass (Da):11,004
Last modified:May 30, 2000 - v2
Checksum:iF2504DB8AAC2DD17
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VKRX-ray2.01A/B/C/D/E/F/G1-103[»]
ProteinModelPortaliP49949.
SMRiP49949. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP49949.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR009157. Fd_Zn-bd.
[Graphical view]
PfamiPF13187. Fer4_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000068. Zn_Fdx_Sulfol. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Di-cluster, seven iron ferredoxins from hyperthermophilic Sulfolobales."
    Gomes C.M., Faria A., Carita J.C., Mendes J., Regalla M., Chicau P., Huber H., Stetter K.O., Teixeira M.
    J. Biol. Inorg. Chem. 3:499-507(1998)
    Cited for: PROTEIN SEQUENCE, METHYLATION AT LYS-29 AND LYS-101.
  2. "A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens."
    Teixeira M., Batista R., Campos A.P., Gomes C., Mendes J., Pacheco I., Anemuller S., Hagen W.R.
    Eur. J. Biochem. 227:322-327(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-50.
    Strain: Lei 10 / DSM 3772 / JCM 9191.
  3. "Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins."
    Bentrop D., Bertini I., Lucinat C., Mendes J., Piccioli M., Teixeira M.
    Eur. J. Biochem. 236:92-99(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
    Strain: Lei 10 / DSM 3772 / JCM 9191.

Entry informationi

Entry nameiFER_ACIAM
AccessioniPrimary (citable) accession number: P49949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: October 14, 2015
This is version 78 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, 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.