Reviewed, UniProtKB/Swiss-Prot Q9XDB2 (DSBD_PANCI)

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

Organism

Pantoea citrea

Taxonomic identifier

53336 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

Protein attributes

Sequence length	578 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
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 – 578	556	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_0000007379
Regions
	Topological domain	23 – 180	158	Periplasmic Potential
	Transmembrane	181 – 201	21	Potential
	Topological domain	202 – 216	15	Cytoplasmic Potential
	Transmembrane	217 – 237	21	Potential
	Topological domain	238 – 253	16	Periplasmic Potential
	Transmembrane	254 – 274	21	Potential
	Topological domain	275 – 306	32	Cytoplasmic Potential
	Transmembrane	307 – 327	21	Potential
	Topological domain	328 – 336	9	Periplasmic Potential
	Transmembrane	337 – 357	21	Potential
	Topological domain	358 – 367	10	Cytoplasmic Potential
	Transmembrane	368 – 388	21	Potential
	Topological domain	389 – 394	6	Periplasmic Potential
	Transmembrane	395 – 415	21	Potential
	Topological domain	416 – 428	13	Cytoplasmic Potential
	Transmembrane	429 – 449	21	Potential
	Topological domain	450 – 578	129	Periplasmic Potential
	Domain	436 – 577	142	Thioredoxin
Amino acid modifications
	Disulfide bond	125 ↔ 131		Redox-active By similarity
	Disulfide bond	193 ↔ 315		Redox-active By similarity
	Disulfide bond	492 ↔ 495		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XDB2-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 383B32797B7FA0E4	FASTA	578	62,547
	10 20 30 40 50 60 MVARLTRLII LALTLFSLHA QAGLFDSGSS PHFVTVNQAF GFDFSQNNHN VVLRWKVKPG 70 80 90 100 110 120 YYLYRQQFSI TGTNAVIAGI ALPSGQPHED EFFGKSQIFP QDVQIPVTLK STLPGATLKI 130 140 150 160 170 180 SYQGCAAAGF CYPPETREVP LSQVSTTRSE APATAAATPA PVPEPQSGPA VSRLPFSPLW 190 200 210 220 230 240 ALLIGIGIAF TPCVLPMYPL ISAIILGGRR DVRASRILLL AFVYVQGMGL TYTLMGIVVA 250 260 270 280 290 300 AAGLRFQAAL QSPVILLSLS AVFILLALSM FGLFSLQLPS SLQTRLTLWS NRQQGGSLSG 310 320 330 340 350 360 VFLMGALAGL ICSPCTTAPL SAILLYIAQS GNMLAGGGTL YLYALGMGLP LIIVTLFGNK 370 380 390 400 410 420 LLPKSGPWMQ SVKEGFGFVI LALPVFLIDR VAGDLWGMRL WSLLGVAFFG WAFALSLKSP 430 440 450 460 470 480 KGWMRVLQIV WLLAALVAAR PLQDWAFATP GVTASQEQAL PFQNIGTVAD LQQQLSQAQG 490 500 510 520 530 540 KITMVDLYAD WCVACKEFEK YTFTDPQVRQ EFSQFRLVQA NVTANSAQDN ALLTHLNVLG 550 560 570 LPTLLFFDAN GHEIPDSRVT GYMNASQFLA HLRKLRAE

References

[1]	"Genetic and biochemical characterization of the pathway in Pantoea citrea leading to pink disease of pineapple." Pujol C.J., Kado C.I. J. Bacteriol. 182:2230-2237(2000) [PubMed: 10735866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1056R.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF102175 Genomic DNA. Translation: AAD38449.1.
3D structure databases
HSSP	HSSP built from PDB template 1JPE based on UniProtKB P36655.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.8. 295631.
Family and domain databases
HAMAP	MF_00399. [Tree]
InterPro	IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. 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. [Graphical view]
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DSBD_PANCI

Accession

Primary (citable) accession number: Q9XDB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 58 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)