NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.21.7292-7308.2005; PubMed=16237012 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.;
"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species.";
J. Bacteriol. 187:7292-7308(2005).

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

AP006716; BAE03541.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_252147.1; -.

3D structure databases

ModBase

Q4L9Y4.

Enzyme and pathway databases

BioCyc

SHAE279808:SH0232-MON; -.

Ontologies

GO:0008926;	Molecular function: mannitol-1-phosphate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
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.

BLOCKS

Q4L9Y4.

Genome annotation databases

3482068; -.

AP006716_GR; SH0232.

sha:SH0232; -.

fig|279808.3.peg.245; -.

Phylogenomic databases

HOGENOM

Q4L9Y4; -.

Genome annotation databases

CMR

Q4L9Y4; SH0232.

Other

ProtoNet

Q4L9Y4.

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`	`1 367`	`367`	`Mannitol-1-phosphate 5-dehydrogenase.`	`PRO_1000011816`
`NP_BIND`	`3 14`	`12`	`NAD (By similarity).`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 41093 Da [This is the MW of the unprocessed precursor]

CRC64: ECC9EF1D8614487F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAVHFGAGN IGRGFIGYIL SDNNIDVTFA DVNEEIINAL DNEGAYNVIL ANEEKTTTRV 

        70         80         90        100        110        120 
TGVSAINSGQ LSDELKQAIL EADIITTAVG VNILPIIAKS FAPVLKEKEN HVNIVACENA 

       130        140        150        160        170        180 
IMATDTLKEA ILDITGPLGD NIHFANSAVD RIVPLQKNDN ILDVMVEPFF EWVVEKDAWY 

       190        200        210        220        230        240 
GEELEHIKYV DDLTPYIERK LLTVNTGHAL LAYAGRFYGR DTVLDAVKDE AIVADLRQVL 

       250        260        270        280        290        300 
GETSEYIVDN FSFTKEEQAA YVEKIIGRFE NPYLSDEVTR VGRGTIRKIG PKDRIIKPLS 

       310        320        330        340        350        360 
YLYENNLRRK GLLKAAALLL KYDDMNDKET IEMREYIDAH GVKAFLQEYA KINDRLADEI 


VAVYEDL

Q4L9Y4 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