NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, AND SUBUNIT.
DOI=10.1074/jbc.274.17.11761; PubMed=10206992 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y.;
"Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.";
J. Biol. Chem. 274:11761-11767(1999).

Comments

FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity).
CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = oxaloacetate + NADH.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 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

AF109682; AAD13225.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1B8P; X-ray; 1.90 A; A=1-329.	[ExPASy / RCSB / EBI]
1B8U; X-ray; 2.50 A; A=1-329.	[ExPASy / RCSB / EBI]
1B8V; X-ray; 2.10 A; A=1-329.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B8P; -.
1B8U; -.
1B8V; -.

ModBase

Q9ZF99.

Ontologies

GO:0030060;	Molecular function: L-malate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01517; -; 1.
PBIL [Tree]

InterPro

IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010945; Malate_DHase_SF1.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR23382; MDH_SF1; 1.

Pfam

PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000102; Lac_mal_DH; 1.

ProDom

PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01759; MalateDH-SF1; 1.

PROSITE

PS00068; MDH; FALSE_NEG.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 329`	`328`	`Malate dehydrogenase.`	`PRO_0000113346`
`NP_BIND`	`12 18`	`7`	`NAD.`
`NP_BIND`	`132 134`	`3`	`NAD.`
`ACT_SITE`	`190 190`		`Proton acceptor.`
`BINDING`	`95 95`		`Substrate (By similarity).`
`BINDING`	`101 101`		`Substrate (By similarity).`
`BINDING`	`108 108`		`NAD (By similarity).`
`BINDING`	`115 115`		`NAD.`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`165 165`		`Substrate.`
`STRAND`	`6 12`	`7`
`HELIX`	`16 26`	`11`
`TURN`	`27 31`	`5`
`STRAND`	`37 42`	`6`
`HELIX`	`47 61`	`15`
`TURN`	`62 64`	`3`
`STRAND`	`68 76`	`9`
`HELIX`	`77 80`	`4`
`TURN`	`81 83`	`3`
`STRAND`	`85 89`	`5`
`HELIX`	`101 122`	`22`
`STRAND`	`128 131`	`4`
`STRAND`	`133 135`	`3`
`HELIX`	`136 145`	`10`
`HELIX`	`152 154`	`3`
`STRAND`	`155 157`	`3`
`HELIX`	`160 174`	`15`
`HELIX`	`178 180`	`3`
`STRAND`	`181 183`	`3`
`STRAND`	`185 188`	`4`
`STRAND`	`195 197`	`3`
`HELIX`	`208 212`	`5`
`HELIX`	`215 220`	`6`
`HELIX`	`222 227`	`6`
`HELIX`	`229 237`	`9`
`HELIX`	`242 258`	`17`
`STRAND`	`265 270`	`6`
`HELIX`	`274 276`	`3`
`STRAND`	`282 290`	`9`
`STRAND`	`293 296`	`4`
`HELIX`	`304 324`	`21`
`HELIX`	`325 328`	`4`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35251 Da [This is the MW of the unprocessed precursor]

CRC64: F02E2826E5028F27 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ KALQGVMMEI 

        70         80         90        100        110        120 
DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME RKDLLEANAQ IFTVQGKAID 

       130        140        150        160        170        180 
AVASRNIKVL VVGNPANTNA YIAMKSAPSL PAKNFTAMLR LDHNRALSQI AAKTGKPVSS 

       190        200        210        220        230        240 
IEKLFVWGNH SPTMYADYRY AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS 

       250        260        270        280        290        300 
SAASAANAAI DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL 

       310        320 
SIDAFSQERI NVTLNELLEE QNGVQHLLG

Q9ZF99 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