NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2007-8-6-r103; PubMed=17550610 [NCBI, ExPASy, EBI, Israel, Japan]
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.;
"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains.";
Genome Biol. 8:RESEARCH103.1-RESEARCH103.18(2007).

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.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (By similarity).
SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000671; ABQ98840.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001291223.1; -.

3D structure databases

ModBase

A5UDI9.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0047134;	Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from HAMAP).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0017004;	Biological process: cytochrome complex assembly (inferred from electronic annotation from HAMAP).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00399; -; 1.
PBIL [Tree]

InterPro

IPR003834; Cyt_c_assmbl_TM.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF02683; DsbD; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.

PROSITE

PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

5226086; -.

GenomeReviews

CP000671_GR; CGSHiEE_07605.

KEGG

hip:CGSHiEE_07605; -.

CMR

A5UDI9; CGSHiEE_07605.

Other

ProtoNet

A5UDI9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Cytochrome c-type biogenesis; Electron transport; Membrane; NAD; Oxidoreductase; Redox-active center; Signal; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`CHAIN`	`17 579`	`563`	`Thiol:disulfide interchange protein dsbD.`	`PRO_1000049609`
`TRANSMEM`	`178 198`	`21`	`Potential.`
`TRANSMEM`	`230 250`	`21`	`Potential.`
`TRANSMEM`	`254 274`	`21`	`Potential.`
`TRANSMEM`	`296 316`	`21`	`Potential.`
`TRANSMEM`	`337 357`	`21`	`Potential.`
`TRANSMEM`	`376 396`	`21`	`Potential.`
`TRANSMEM`	`397 417`	`21`	`Potential.`
`TRANSMEM`	`420 440`	`21`	`Potential.`
`DOMAIN`	`449 579`	`131`	`Thioredoxin.`
`DISULFID`	`124 129`		`Redox-active (By similarity).`
`DISULFID`	`193 315`		`Redox-active (By similarity).`
`DISULFID`	`495 498`		`Redox-active (By similarity).`

Sequence information

Length: 579 AA [This is the length of the unprocessed precursor]

Molecular weight: 64505 Da [This is the MW of the unprocessed precursor]

CRC64: 12B4D67BC4FAA107 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDITDGYYL 

        70         80         90        100        110        120 
YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGTF NNADDKVEIT 

       130        140        150        160        170        180 
YQGCTEGFCY PPETKVLRIG DLAISQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWTIFG 

       190        200        210        220        230        240 
FFLLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA 

       250        260        270        280        290        300 
AIGLPFQIAL QHPYVMIGLS ILFVVLALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG 

       310        320        330        340        350        360 
AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAATL YLLALGMGVP LMLITLFGNK 

       370        380        390        400        410        420 
ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWEPRL WAGLATVFFI WFALQMSKNG 

       430        440        450        460        470        480 
FGYAIKIISF VLAMVTVQPL QNWIWQTQTT TQSAVENKSV SQVKFKQIKN TEELDRTLAE 

       490        500        510        520        530        540 
NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVNMTKNSP ENKALMERFN 

       550        560        570 
VMGLPTILFF DQQNNEIKGS RVTGFMDADA FSNWLKALH

A5UDI9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools