Reviewed, UniProtKB/Swiss-Prot Q5QVU3 (DSBD_IDILO)

Names and origin

Protein names

Recommended name:
    Thiol:disulfide interchange protein dsbD
    EC=1.8.1.8
Alternative name(s):
    Protein-disulfide reductase
      Short name=Disulfide reductase

Gene names

Name:	dsbD
Ordered Locus Names:	IL2283

Organism

Idiomarina loihiensis [Complete proteome] [HAMAP]

Taxonomic identifier

135577 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps By similarity.
Catalytic activity	Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP MF_00399
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the thioredoxin family. DsbD subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis Electron transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center Signal Transmembrane
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cytochrome complex assembly Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: HAMAP protein-disulfide reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 568	546	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_0000304390
Regions
	Transmembrane	172 – 192	21	Potential
	Transmembrane	215 – 235	21	Potential
	Transmembrane	250 – 270	21	Potential
	Transmembrane	294 – 314	21	Potential
	Transmembrane	332 – 352	21	Potential
	Transmembrane	364 – 384	21	Potential
	Transmembrane	392 – 412	21	Potential
	Transmembrane	418 – 438	21	Potential
	Domain	416 – 567	152	Thioredoxin
Amino acid modifications
	Disulfide bond	128 ↔ 134		Redox-active By similarity
	Disulfide bond	190 ↔ 311		Redox-active By similarity
	Disulfide bond	482 ↔ 485		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5QVU3-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 7D26ABB10295C0C4	FASTA	568	62,859
	10 20 30 40 50 60 MIQRFITCLA ALTLVFAVVA PAHSVQSNPF QQDNQFLSVD QAFDFDSEVN DSKVTVSWVV 70 80 90 100 110 120 APEYYLYQHR FKVVPENALA AEPELPQGES HNDEFFGESI VYRNYVEWSF TLNPEFSGDT 130 140 150 160 170 180 ITVQYQGCAD AGLCYPPTEK QIKLSSTSET APATAPPNTD SSLFGIGEQH LIITLLLFFA 190 200 210 220 230 240 LGIGLAFTPC VFPMYPILSG VVLGNRERNW KNTLWLSFIY VQGMAITYSL LGLVVASAGM 250 260 270 280 290 300 QYQAYFQHPV VLIVLAVLFA LFALSMFGAY TLQLPISWQS KLQSFSGQQS GGNIVGVFII 310 320 330 340 350 360 GAISGLVASP CTTAPLSGAL LFIAQSGDMV SGVAILYALS LGMGVPLILF GLSGGKLLPK 370 380 390 400 410 420 AGAWMNVVKQ FFGWLLLAVT LFLIERLIPT SISMWLWIFY FILAAVSLAV SISQPLRITT 430 440 450 460 470 480 KVITIVLLAA AATTGSYWQV NKAQLEQKSH GLFTVVSNVS DIQQQVAESD RWVMLDLYAD 490 500 510 520 530 540 WCVACKEFEQ YTFSDEQVQA QFQEFKLIQA DVTRNNAQDV EILSRYKVLG LPTILFFDPE 550 560 GNERPEYRVT GYMNAEDFKK HLEKIVSE

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L2-TR / ATCC BAA-735 / DSM 15497.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017340 Genomic DNA. Translation: AAV83115.1.
RefSeq	YP_156664.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3173543.
GenomeReviews	Gene locus IL2283 in contig AE017340_GR.
KEGG	ilo:IL2283.
NMPDR	fig|283942.3.peg.2270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5QVU3.
OMA	Q5QVU3. LIVGACS.
Enzyme and pathway databases
BioCyc	ILOI283942:IL2283-MON.
BRENDA	1.8.1.8. 280818.
Family and domain databases
HAMAP	MF_00399. [Tree]
InterPro	IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR10438. Trx. 1 hit.
Pfam	PF02683. DsbD. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DSBD_IDILO

Accession

Primary (citable) accession number: Q5QVU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	January 4, 2005
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)