NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/1471-2164-7-173; PubMed=16822325 [NCBI, ExPASy, EBI, Israel, Japan]
Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a.";
BMC Genomics 7:173-173(2006).

Comments

CATALYTIC ACTIVITY: D-altronate + NAD⁺ = D-tagaturonate + NADH.
PATHWAY: Carbohydrate metabolism; pentose and glucuronate interconversion .
SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB subfamily.

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

CP000266; ABF03757.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_689062.1; -.

3D structure databases

ModBase

Q0T4K8.

Enzyme and pathway databases

BioCyc

SFLE373384:SFV_1580-MON; -.

Ontologies

GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0009026;	Molecular function: tagaturonate reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00670; -; 1.
PBIL [Tree]

InterPro

IPR013328; DHase_multihelical.
IPR013118; Mannitol_DHase_C.
IPR013131; Mannitol_DHase_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF01232; Mannitol_dh; 1.
PF08125; Mannitol_dh_C; 1.
Pfam graphical view of domain structure.

ProtoNet

Q0T4K8.

Genome annotation databases

GeneID

4208035; -.

GenomeReviews

CP000266_GR; SFV_1580.

KEGG

sfv:SFV_1580; -.

Phylogenomic databases

HOGENOM

Q0T4K8; -.

Genome annotation databases

CMR

Q0T4K8; SFV_1580.

Other

UniRef

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

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 483`	`483`	`Altronate oxidoreductase.`	`PRO_1000044707`
`NP_BIND`	`18 29`	`12`	`NAD (By similarity).`

Sequence information

Length: 483 AA [This is the length of the unprocessed precursor]

Molecular weight: 54856 Da [This is the MW of the unprocessed precursor]

CRC64: AFA4677CE3B5CC10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP 

        70         80         90        100        110        120 
SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN 

       130        140        150        160        170        180 
TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL 

       190        200        210        220        230        240 
RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT 

       250        260        270        280        290        300 
AEHFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG 

       310        320        330        340        350        360 
LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA 

       370        380        390        400        410        420 
LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER 

       430        440        450        460        470        480 
YQQLWSQHRD RVIGTQELVA IVLAEKYHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR 


PLC

Q0T4K8 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