Reviewed, UniProtKB/Swiss-Prot P42734 (MTDH_ARATH)

Names and origin

Protein names

Recommended name:
    Probable mannitol dehydrogenase
    EC=1.1.1.255
Alternative name(s):
    NAD-dependent mannitol dehydrogenase

Gene names

Name:	CAD1
Ordered Locus Names:	At4g39330
ORF Names:	T22F8.230

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level By similarity.
Catalytic activity	D-mannitol + NAD+ = D-mannose + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
Caution	Was originally (Ref.1) thought to be a cinnamyl-alcohol dehydrogenase.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR
Molecular function	mannitol dehydrogenase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449530,EBI-449157

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P42734-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	Probable mannitol dehydrogenase		PRO_0000160810
Sites
	Metal binding	50	1	Zinc 1; catalytic By similarity
	Metal binding	72	1	Zinc 1; catalytic By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	109	1	Zinc 2 By similarity
	Metal binding	117	1	Zinc 2 By similarity
	Metal binding	166	1	Zinc 1; catalytic By similarity
Experimental info
	Sequence conflict	202	1	I → S in AAA99511. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: 0E4F3B0581785759	FASTA	360	38,934
	10 20 30 40 50 60 MAKSPETEHP NKVFGWGARD KSGVLSPFHF SRRDNGENDV TVKILFCGVC HTDLHTIKND 70 80 90 100 110 120 WGYSYYPVVP GHEIVGIATK VGKNVTKFKE GDRVGVGVIS GSCQSCESCD QDLENYCPQM 130 140 150 160 170 180 SFTYNAIGSD GTKNYGGYSE NIVVDQRFVL RFPENLPSDS GAPLLCAGIT VYSPMKYYGM 190 200 210 220 230 240 TEAGKHLGVA GLGGLGHVAV KIGKAFGLKV TVISSSSTKA EEAINHLGAD SFLVTTDPQK 250 260 270 280 290 300 MKAAIGTMDY IIDTISAVHA LYPLLGLLKV NGKLIALGLP EKPLELPMFP LVLGRKMVGG 310 320 330 340 350 360 SDVGGMKETQ EMLDFCAKHN ITADIELIKM DEINTAMERL AKSDVRYRFV IDVANSLSPP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana." Somers D.A., Nourse J.P., Manners J.M., Abrahams S.L., Watson J.M. Plant Physiol. 108:1309-1310(1995) [PubMed: 7630954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37883 Genomic DNA. Translation: AAA99511.1. L37884 mRNA. Translation: AAA74746.1. AL050351 Genomic DNA. Translation: CAB43648.1. AL161595 Genomic DNA. Translation: CAB80596.1. AF370498 mRNA. Translation: AAK43875.1. AY064669 mRNA. Translation: AAL47376.1. AY302076 mRNA. Translation: AAP59429.1.
IPI	IPI00540521.
PIR	S71179. T08581.
RefSeq	NP_195643.1.
UniGene	At.24772 At.65473 At.67820
3D structure databases
HSSP	HSSP built from PDB template 1UUF based on UniProtKB P75691.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42734. 1 interaction.
Proteomic databases
PRIDE	P42734.
Genome annotation databases
GeneID	830088.
GenomeReviews	Gene locus AT4G39330 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.22068.
Organism-specific databases
TAIR	At4g39330.
Phylogenomic databases
OMA	P42734. RIVSISI.
Enzyme and pathway databases
BRENDA	1.1.1.255. 302.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTDH_ARATH

Accession

Primary (citable) accession number: P42734
Secondary accession number(s): Q94K02

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 29, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)