Q8GPG4 (DDHA_RHOSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethylsulfide dehydrogenase subunit alpha
EC=1.8.2.4

Alternative name(s):
DMS DH molybdenum subunit
DMS DH subunit alpha
Dimethyl sulfide:cytochrome c2 reductase subunit alpha
Dimethylsulfide dehydrogenase molybdenum subunit

Gene names

Name:

ddhA

Organism

Rhodovulum sulfidophilum (Rhodobacter sulfidophilus)

Taxonomic identifier

35806 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	910 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Allows photoautotrophic growth on dimethyl sulfide (DMS) as the sole electron donor. Ref.2
Catalytic activity	Dimethyl sulfide + 2 ferricytochrome c2 + H2O = dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+. Ref.2
Cofactor	Binds 1 4Fe-4S cluster Potential. Ref.2 Molybdenum (molybdopterin). Ref.2
Subunit structure	Heterotrimer of alpha, beta and gamma subunits. Ref.2
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity 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
	Signal peptide	1 – 28	28	Tat-type signal Ref.1
	Chain	29 – 910	882	Dimethylsulfide dehydrogenase subunit alpha		PRO_0000019174
Regions
	Domain	59 – 123	65	4Fe-4S Mo/W bis-MGD-type
Sites
	Metal binding	66	1	Iron-sulfur (4Fe-4S); via pros nitrogen By similarity
	Metal binding	70	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	74	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	109	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8GPG4 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 8332BC7C8D8F25FB	FASTA	910	102,309
	10 20 30 40 50 60 MLRTTRRTLM QGASLVGAGL FAAGRGWALN RLEPIGDTLA EEYPYRDWED LYRNEFTWDY 70 80 90 100 110 120 VGKAAHCINC LGNCAFDIYV KDGIVIREEQ LAKYPQISPD IPDANPRGCQ KGAIHSTSMY 130 140 150 160 170 180 EADRLRYPMK RVGARGEGKW QRISWDQATE EIADKIIDIY EKYGPGKLMT HTGSGNMSMM 190 200 210 220 230 240 RMAAPYRFAS LVGGVQLDIF TDVGDLNTGA HLAYGNALES FTSDAWFGAD YIMFLLFNPV 250 260 270 280 290 300 ATRIPDAHFL WEAKWNGARV VSVAPDYNPS SIHSDLWMPI KQGADPFLAM SMVNVIIEGK 310 320 330 340 350 360 LYNEAFMKEQ TDLPILVRSD NGMLLREADL EEGGSDQVFY HWDSRTGAAV KVKGSMGSEE 370 380 390 400 410 420 KTLVLGDVDP ALEGSFEVGG IPVTTVFEKV RAEAAKYPPE ETAAITGIGP GVVRAEAETF 430 440 450 460 470 480 ARAKKALLMT GFNIGRYSNG IYTSWALTLM LALTGHGGRT GGLDTSWIAW NQPALLELAF 490 500 510 520 530 540 FDFKKLPRLE AGGLGEFVRG GMMEHSRQHY DNDKLKARTG FDLDELQEMI DESIDAGWMP 550 560 570 580 590 600 YYGDMKGLIS IADNKFRRNK NAEAYRERIL EEVEELFVDI NVRMDSTAQW ADYLLPAAAH 610 620 630 640 650 660 YEAWDLRSIA FHRFVNVFSR PVPPIGEAKS DWEIMEILTR KIQERAIARG ITGYEDGDVT 670 680 690 700 710 720 RDFATIHDDY TMDGTLMTDH DVVSWLVENG PEFAGATLEE GVERGFFVMG EDAGPTQKLR 730 740 750 760 770 780 PSEPYHAFLQ QTEGKEPYKT MTGRITFFVD HPRFVRLGAT VPTARHHAGR DASNYPLNFF 790 800 810 820 830 840 SPHTRWGIHS NWRSNKFMLR LQRGEPNIYI SPQLAAAKGI ADGAQVRVFN ELSFFFAQAK 850 860 870 880 890 900 FYPSLPPDTI MMEHGWEPHQ FPNWRPMNVC MATLLQPLEL VGGWGHLNFS LWHWNANQLA 910 HESSVDIEPA

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], PROTEIN SEQUENCE OF 29-38. 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: CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF453479 Genomic DNA. Translation: AAN46632.1.
3D structure databases
ProteinModelPortal	Q8GPG4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14242.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR017840. DMSO_Rdtase_II_Mopterin_su. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006311. TAT_signal. [Graphical view]
Pfam	PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR03479. DMSO_red_II_alp. 1 hit.
PROSITE	PS51669. 4FE4S_MOW_BIS_MGD. 1 hit. PS00551. MOLYBDOPTERIN_PROK_1. False negative. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DDHA_RHOSU

Accession

Primary (citable) accession number: Q8GPG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	May 29, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program