Reviewed, UniProtKB/Swiss-Prot P16468 (MAOX_BACST)

Names and origin

Protein names	Recommended name:     NAD-dependent malic enzyme       Short name=NAD-ME     EC=1.1.1.38
Organism	Bacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier	1422 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 structure	Homotetramer.
Miscellaneous	This enzyme has a higher affinity for NAD than for NADP.
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Ligand	Metal-binding NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	NAD-dependent malic enzyme		PRO_0000160207
Regions
	Nucleotide binding	151 – 158	8	NAD By similarity
Sites
	Active site	114	1	Proton donor By similarity
	Active site	169	1	Proton acceptor By similarity
	Metal binding	211	1	Divalent metal cation By similarity
	Metal binding	212	1	Divalent metal cation By similarity
	Binding site	237	1	NAD By similarity
	Binding site	363	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P16468-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 8CE6629A2E6AFE74	FASTA	478	51,537
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	M19485 Genomic DNA. Translation: AAA22585.1.
PIR	DEBSXS. A33307.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.38. 266715.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01842. ACT. 1 hit. PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAOX_BACST

Accession

Primary (citable) accession number: P16468

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)