[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2644282 [NCBI, ExPASy, EBI, Israel, Japan] Kobayashi K., Doi S., Negoro S., Urabe I., Okada H.; "Structure and properties of malic enzyme from Bacillus stearothermophilus."; J. Biol. Chem. 264:3200-3205(1989).

Comments

FUNCTION: In addition to the NAD-dependent oxidative decarboxylation of L-malate, the enzyme catalyzes the decarboxylation of oxaloacetate.
CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = pyruvate + CO₂ + NADH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese. The activity is enhanced 5-7 times by ammonium and potassium.
SUBUNIT: Homotetramer.
MISCELLANEOUS: This enzyme has a higher affinity for NAD than for NADP.
SIMILARITY: Belongs to the malic enzymes 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

M19485; AAA22585.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A33307; DEBSXS.

3D structure databases

ModBase

P16468.

Family and domain databases

InterPro

IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.

PROSITE

PS00331; MALIC_ENZYMES; 1.

Other

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

Keywords

Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 478`	`478`	`NAD-dependent malic enzyme.`	`PRO_0000160207`
`NP_BIND`	`151 158`	`8`	`NAD (By similarity).`
`ACT_SITE`	`114 114`		`Proton donor (By similarity).`
`ACT_SITE`	`169 169`		`Proton acceptor (By similarity).`
`METAL`	`211 211`		`Divalent metal cation (By similarity).`
`METAL`	`212 212`		`Divalent metal cation (By similarity).`
`BINDING`	`237 237`		`NAD (By similarity).`
`BINDING`	`363 363`		`NAD (By similarity).`

Sequence information

Length: 478 AA [This is the length of the unprocessed precursor]

Molecular weight: 51537 Da [This is the MW of the unprocessed precursor]

CRC64: 8CE6629A2E6AFE74 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALPGGAAMN ITIRLQFEKD IVSFSDIAAA IGKAGGDIVG IDVISSSKVH TVRDITVSAL 

        70         80         90        100        110        120 
DTKQCDLIIE ALKKIRGVKI VNVSDRTFLM HIGGKIETNS KIPVKTRDDL SRVYTPGVAR 

       130        140        150        160        170        180 
VCTAIAEDPR KAYSLTIKRN TVAVVSDGTA VLGLGDIGPY AAMPVMEGKA MLFKEFAGVD 

       190        200        210        220        230        240 
AFPICLDTKD TEEIIQIVKA IAPAFGGINL EDISAPRCFE IEKRLKEELD IPVFHDDQHG 

       250        260        270        280        290        300 
TAVVLLAGLL NALKIVDKKL EDIKVVLTGI GAAGIACTKI LLAAGVRNII GVDRHGAIHR 

       310        320        330        340        350        360 
DETYENPYWQ EYAQLTNPDN LKGSLSDVIA GADVFIGVSA PGILKVEDVK KMARDPIVFA 

       370        380        390        400        410        420 
MANPIPEIDP ELAEPYVRVM ATGRSDYPNQ INNVLCFPGI FRGALDCRAR EINEEMKLAA 

       430        440        450        460        470 
AKAIASVVTE DELNETYIIP SVFNSKVVER VRQAVVEAAY RTGVARKDNI PVGGYTGQ

P16468 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