[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1371/journal.pone.0001120; PubMed=17971880 [NCBI, ExPASy, EBI, Israel, Japan] Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.; "Molecular correlates of host specialization in Staphylococcus aureus."; PLoS ONE 2:E1120-E1120(2007).

Comments

CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD⁺ = D-fructose 6-phosphate + NADH.
SIMILARITY: Belongs to the mannitol dehydrogenase family.

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

AJ938182; CAI81728.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_417497.1; -.

3D structure databases

ModBase

Q2YYE8.

Enzyme and pathway databases

BioCyc

SAUR273036:SAB2039-MON; -.

Ontologies

GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0008926;	Molecular function: mannitol-1-phosphate 5-dehydrogenase 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_00196; -; 1.
PBIL [Tree]

InterPro

IPR013328; DHase_multihelical.
IPR013118; Mannitol_DHase_C.
IPR000669; Mannitol_DHase_core.
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.

PRINTS

PR00084; MTLDHDRGNASE.

PROSITE

PS00974; MANNITOL_DHGENASE; 1.

Genome annotation databases

GeneID

3793464; -.

GenomeReviews

AJ938182_GR; SAB2039.

KEGG

sab:SAB2039; -.

NMPDR

fig|273036.3.peg.1978; -.

Phylogenomic databases

HOGENOM

Q2YYE8; -.

Genome annotation databases

CMR

Q2YYE8; SAB2039.

Other

ProtoNet

Q2YYE8.

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`	`1 368`	`368`	`Mannitol-1-phosphate 5-dehydrogenase.`	`PRO_1000011815`
`NP_BIND`	`3 14`	`12`	`NAD (By similarity).`

Sequence information

Length: 368 AA [This is the length of the unprocessed precursor]

Molecular weight: 40980 Da [This is the MW of the unprocessed precursor]

CRC64: FE95E2ED69A21ACB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAVHFGAGN IGRGFIGYIL ADNNVKVTFA DVNEEIINAL AHDHQYDVIL ADESKTTTRV 

        70         80         90        100        110        120 
NNVDAINSMQ PSEALKQAIL EGDIITTAVG VNILPIIAKS FAPFLKEKTN HVNIVACENA 

       130        140        150        160        170        180 
IMATDTLKKA VLDITGPLGN NIHFANSAVD RIVPLQKNEN ILDVMVEPFY EWVVEKDAWY 

       190        200        210        220        230        240 
GPELNHIKYV DDLTPYIERK LLTVNTGHAY LAYAGKFADK ATVLDAVKDS SIEAGLRRVL 

       250        260        270        280        290        300 
AETSQYITNE FDFTEAEQAG YVEKIIDRFN NSYLSDEVTR VGRGTLRKIG PKDRIIKPLT 

       310        320        330        340        350        360 
YLYNKDLERT GLLNTAALLL KYDDTADQET VEKNNYIKEH GLKAFLSEYA KVDDGLADEI 


IEAYNSLS

Q2YYE8 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