Diheme cytochrome c - Rhodovulum sulfidophilum

Preferred order of sections

Names and origin

Protein names

Submitted name:
Diheme cytochrome c EMBL AAF99434.1

Gene names

Name:

soxA EMBL AAF99434.1

Organism

Rhodovulum sulfidophilum (Rhodobacter sulfidophilus) EMBL AAF99434.1

Taxonomic identifier

35806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodovulum

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Heme PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1 Iron Metal-binding
Technical term	3D-structure PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1
Gene Ontology (GO)
Cellular_component	cytochrome complex Inferred from electronic annotation. Source: InterPro
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

106

1

Iron (heme 2 axial ligand); via tele nitrogen PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Metal binding

140

1

Iron (heme 2 axial ligand) PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Metal binding

207

1

Iron (heme 1 axial ligand); via tele nitrogen PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Metal binding

248

1

Iron (heme 1 axial ligand) PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Binding site

102

1

Heme 2 (covalent) PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Binding site

105

1

Heme 2 (covalent) PDB 1H32 PDB 1H31 PDB 1H33

Binding site

203

1

Heme 1 (covalent) PDB 1H32 PDB 1H31 PDB 1H33

Binding site

206

1

Heme 1 (covalent) PDB 1H32 PDB 1H31 PDB 1H33

Amino acid modifications

Modified residue

248

1

Cysteine persulfide PDB 1H32 PDB 1H31 PDB 1H33 PDB 2OZ1

Sequences

Sequence

Length

Mass (Da)

Tools

Q939U1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 95748C569D40853F
Show »

FASTA

287

31,332

        10         20         30         40         50         60 
MKTMTGRLVA AALVCGGAFS GAAVSAGPDD PLVINGEIEI VTRAPTPAHL ADRFDEIRSG 

        70         80         90        100        110        120 
WTFRTDDTQA LEMDDFENSG MVFVEEARAV WDRPEGTEGK ACADCHGAVD DGMYGLRAVY 

       130        140        150        160        170        180 
PKYVESAGKV RTVEQMINAC RTSRMGAPEW DYIGPDMTAM VALIASVSRG MPVSVAIDGP 

       190        200        210        220        230        240 
AQSTWEKGRE IYYTRYGQLD LSCASCHEQY FDHYIRADHL SQGQINGFPS YRLKNARLNA 

       250        260        270        280 
VHDRFRGCIR DTRGVPFAVG SPEFVALELY VASRGNGLSV EGPSVRN

« Hide

References

[1]	"Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum." Appia-Ayme C., Little P.J., Matsumoto Y., Leech A.P., Berks B.C. J. Bacteriol. 183:6107-6118(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme." Bamford V.A., Bruno S., Rasmussen T., Appia-Ayme C., Cheesman M.R., Berks B.C., Hemmings A.M. EMBO J. 21:5599-5610(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-287 IN COMPLEX WITH HEME, CYSTEINE PERSULFIDE AT CYS-248.
[3]	"The Rhodovulum sulfidophilum sox operon encodes eleven proteins which seem to constitute an oxidation system to metabolize reduced sulfur compounds." Appia-Ayme C., Berks B.C. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	"Two new genes involved in sox locus regulation." Appia-Ayme C., Berks B.C. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[5]	"The crystal structure of recombinant Rhodovulum sulfidophilum SoxAX confirms cysteine persulfide coordination to the catalytic heme." Kihlken M.A., Berks B.C., Hemmings A.M. Submitted (FEB-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-287 IN COMPLEX WITH HEME, CYSTEINE PERSULFIDE AT CYS-248.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY005800 Genomic DNA. Translation: AAF99434.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H31	X-ray	2.55	A/C/E/G	27-287	[»]
1H32	X-ray	1.50	A	27-287	[»]
1H33	X-ray	1.75	A	27-287	[»]
2OZ1	X-ray	2.35	A/C/E/G	27-287	[»]

ProteinModelPortal

Q939U1.

SMR

Q939U1. Positions 27-287.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR009056. Cyt_c_dom.
IPR025710. SoxA.
[Graphical view]

PIRSF

PIRSF038455. SoxA. 1 hit.

SUPFAM

SSF46626. Cytochrome_c. 2 hits.

PROSITE

PS51007. CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q939U1.

Entry information

Entry name

Q939U1_RHOSU

Accession

Primary (citable) accession number: Q939U1

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)