NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RIMD 2210633 / Serotype O3:K6;
DOI=10.1016/S0140-6736(03)12659-1; PubMed=12620739 [NCBI, ExPASy, EBI, Israel, Japan]
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae.";
Lancet 361:743-749(2003).

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

BA000031; BAC58632.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_796748.1; -.

3D structure databases

ModBase

Q87SQ3.

Enzyme and pathway databases

BioCyc

VPAR223926:VP0369-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

Q87SQ3.

Genome annotation databases

1187836; -.

BA000031_GR; VP0369.

vpa:VP0369; -.

fig|223926.1.peg.369; -.

Phylogenomic databases

HOGENOM

Q87SQ3; -.

Genome annotation databases

CMR

Q87SQ3; VP0369.

Other

ProtoNet

Q87SQ3.

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`	`1 382`	`382`	`Mannitol-1-phosphate 5-dehydrogenase.`	`PRO_0000170730`
`NP_BIND`	`4 15`	`12`	`NAD (By similarity).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41978 Da [This is the MW of the unprocessed precursor]

CRC64: 9F5C141DF6769F0F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKNAVHFGAG NIGRGFIGKL LADAEVEVTF ADVDVPLVDQ LSHKQEYKVK VVGTECKIDT 

        70         80         90        100        110        120 
VTHVTAVNSA SEDVIDRIVK TDLVTTAVGP NVLDIIAKTI AKGIAKRFEA GNDAPLNIIA 

       130        140        150        160        170        180 
CENMVRGTTH LKGEVYKHLD KSLHAKADEL VGFVDSAVDR IVPPAEAAND DPLEVTVESF 

       190        200        210        220        230        240 
SEWIVDEQQF KGDIPNIAGM EKTNNLMAFV ERKLFTLNTG HCITAYLGCL KGHRTIREAI 

       250        260        270        280        290        300 
EDPNIHAEVK QAMQESGEVL IRRYGFDHDM HNAYIEKILG RFANPYLVDE VDRVGRQPIR 

       310        320        330        340        350        360 
KLGANDRLVK PLLGTIEYGT ENQTLLKGIA AALKYTNDTD PQAVELQTSL KEVGVTKTLA 

       370        380 
KYTGLAEDSD EVAQIETLYN QL

Q87SQ3 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