Q8GPG3 (DDHB_RHOSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethylsulfide dehydrogenase subunit beta
Short name=DMS DH subunit beta

Alternative name(s):
DMS DH iron-sulfur subunit
Dimethyl sulfide:cytochrome c2 reductase subunit beta
Dimethylsulfide iron-sulfur subunit

Gene names

Name:

ddhB

Organism

Rhodovulum sulfidophilum (Rhodobacter sulfidophilus)

Taxonomic identifier

35806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodovulum

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electron transfer subunit of the dehydrogenase during anaerobic growth on dimethyl sulfide By similarity. Ref.2
Cofactor	Binds 1 3Fe-4S cluster By similarity. Ref.2 Binds 3 4Fe-4S clusters By similarity. Ref.2
Subunit structure	Heterotrimer of alpha, beta and gamma subunits. Ref.2
Subcellular location	Periplasm. Note: Probably translocated together with DdhA, which possesses a Tat-type signal.
Sequence similarities	Contains 3 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Repeat
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Molecule processing
	Chain	1 – 325	325	Dimethylsulfide dehydrogenase subunit beta		PRO_0000159292
Regions
	Domain	6 – 35	30	4Fe-4S ferredoxin-type 1
	Domain	123 – 154	32	4Fe-4S ferredoxin-type 2
	Domain	156 – 185	30	4Fe-4S ferredoxin-type 3
Sites
	Metal binding	15	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	18	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	21	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	25	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	132	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	135	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	140	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	144	1	Iron-sulfur 4 (3Fe-4S) By similarity
	Metal binding	165	1	Iron-sulfur 4 (3Fe-4S) By similarity
	Metal binding	171	1	Iron-sulfur 4 (3Fe-4S) By similarity
	Metal binding	175	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	192	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	195	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	207	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	211	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8GPG3 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: F62990FBD394E727	FASTA	325	37,026
	10 20 30 40 50 60 MVKRQISMVL DLNKCIGCQT CTSACKLQWT NRNGREYMYW NNVETHPGPG YPRNYEHSGG 70 80 90 100 110 120 GFDEEGALKI GITPSAEDYG IPWEYNYEEA LMTGTDPWLR PNVKPTWGAN WNEDEGRGEY 130 140 150 160 170 180 PNSYYFYLPR ICNHCANPGC LAACARNAIY KRQEDGIVLV DQERCRGYRY CITACPYKKV 190 200 210 220 230 240 YFNEQISKAE KCIFCYPRIE KGLPTACAKQ CVGRIRFIGY LDDEAGPVHL LVERYKVAIP 250 260 270 280 290 300 LHPEWGTKPS VFYVPPLAPP RIGDDGEPTE ETRVPLAYLK ELFGEAVVPA LETLKTERAK 310 320 KQSGAESELM DTLIGYRHPE MFKLS

References

[1]	"Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes." McDevitt C.A., Hugenholtz P., Hanson G.R., McEwan A.G. Mol. Microbiol. 44:1575-1587(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SH1.
[2]	"Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor." Hanlon S.P., Toh T.H., Solomon P.S., Holt R.A., McEwan A.G. Eur. J. Biochem. 239:391-396(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF453479 Genomic DNA. Translation: AAN46633.1.
3D structure databases
ProteinModelPortal	Q8GPG3.
SMR	Q8GPG3. Positions 3-323.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14243.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017839. DMSO_Rdtase_II_Fe-S_su. [Graphical view]
Pfam	PF13247. Fer4_11. 1 hit. [Graphical view]
TIGRFAMs	TIGR03478. DMSO_red_II_bet. 1 hit.
PROSITE	PS51379. 4FE4S_FER_2. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DDHB_RHOSU

Accession

Primary (citable) accession number: Q8GPG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program