Reviewed, UniProtKB/Swiss-Prot Q9ZP05 (MDHG1_ARATH)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase, glyoxysomal
    EC=1.1.1.37
Alternative name(s):
    mbNAD-MDH

Gene names

Ordered Locus Names:	At5g09660
ORF Names:	F17I14_150, MTH16.8

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	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH.
Subunit structure	Homodimer By similarity.
Subcellular location	Glyoxysome Potential.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Glyoxysome
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR glyoxysome Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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: Q9ZP05-1)

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
	Transit peptide	1 – 34	34	Glyoxysome Potential
	Chain	35 – 354	320	Malate dehydrogenase, glyoxysomal		PRO_0000018634
Regions
	Nucleotide binding	49 – 55	7	NAD By similarity
	Nucleotide binding	158 – 160	3	NAD By similarity
Sites
	Active site	218	1	Proton acceptor By similarity
	Binding site	75	1	NAD By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	135	1	NAD By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	269	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: AC56EAC7AB025288	FASTA	354	37,369
	10 20 30 40 50 60 MEFRGDANQR IARISAHLTP QMEAKNSVIG RENCRAKGGN PGFKVAILGA AGGIGQSLSL 70 80 90 100 110 120 LMKMNPLVSL LHLYDVVNAP GVTADVSHMD TGAVVRGFLG AKQLEDALTG MDLVIIPAGI 130 140 150 160 170 180 PRKPGMTRDD LFKINAGIVK TLCEGVAKCC PNAIVNLISN PVNSTVPIAA EVFKKAGTYD 190 200 210 220 230 240 PKKLLGVTTL DVARANTFVA EVLGLDPREV DVPVVGGHAG VTILPLLSQV KPPSSFTPQE 250 260 270 280 290 300 IEYLTNRIQN GGTEVVEAKA GAGSATLSMA YAAAKFADAC LRGLRGDANV VECSFVASQV 310 320 330 340 350 TELAFFATKV RLGRTGAEEV YQLGPLNEYE RIGLEKAKDE LAGSIQKGVE FIRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L." Berkemeyer M., Scheibe R., Ocheretina O. J. Biol. Chem. 273:27927-27933(1998) [PubMed: 9774405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S. DNA Res. 6:183-195(1999) [PubMed: 10470850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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	AJ131206 mRNA. Translation: CAA10321.1. AB020752 Genomic DNA. Translation: BAB09521.1. AL353994 Genomic DNA. Translation: CAB89364.1. AF428373 mRNA. Translation: AAL16303.1. AY037252 mRNA. Translation: AAK59853.1. AY077653 mRNA. Translation: AAL76131.1.
IPI	IPI00534849.
PIR	T49932.
RefSeq	NP_196528.1.
UniGene	At.40751 At.47611
3D structure databases
HSSP	HSSP built from PDB template 1MLD based on UniProtKB P00346.
SMR	Q9ZP05. Positions 42-353.
ModBase	Search...
Proteomic databases
PRIDE	Q9ZP05.
ProMEX	Q9ZP05.
Genome annotation databases
GeneID	830825.
GenomeReviews	Gene locus AT5G09660 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.23087.
Organism-specific databases
TAIR	At5g09660.
Phylogenomic databases
OMA	Q9ZP05. ENCRAKG.
Enzyme and pathway databases
BRENDA	1.1.1.37. 302.
Gene expression databases
ArrayExpress	Q9ZP05.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DH. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_NAD-dep_euk_g_bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11540:SF1. MDH_euk_g_bac. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
TIGRFAMs	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDHG1_ARATH

Accession

Primary (citable) accession number: Q9ZP05

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)