O30807 (MAO1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD-dependent malic enzyme
Short name=NAD-ME
EC=1.1.1.39

Gene names

Name:	dme
Ordered Locus Names:	R01837
ORF Names:	SMc00169

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria.
Catalytic activity	(S)-malate + NAD+ = pyruvate + CO2 + NADH.
Cofactor	Divalent metal cations. Prefers magnesium or manganese By similarity.
Enzyme regulation	Subject to substrate inhibition and shows allosteric regulation by acetyl-CoA.
Subunit structure	Homooctamer.
Sequence similarities	In the N-terminal section; belongs to the malic enzymes family. In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.

Ontologies

Keywords
Ligand	Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Allosteric enzyme Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity, transferring acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 770	770	NAD-dependent malic enzyme		PRO_0000160245
Regions
	Region	1 – 440	440	Malic enzyme
	Region	441 – 770	330	Phosphate acetyltransferase
Sites
	Active site	107	1	Proton acceptor By similarity
	Metal binding	149	1	Divalent metal cation By similarity
	Metal binding	150	1	Divalent metal cation By similarity
	Binding site	175	1	NAD By similarity
	Binding site	300	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O30807 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 8FF3E3DA2D923108	FASTA	770	82,865
	10 20 30 40 50 60 MNTGDKAKSQ AVPASGDIDQ QALFFHRYPR PGKLEIQPTK PLGNQRDLAL AYSPGVAAPC 70 80 90 100 110 120 LAIKDNPETA ADFTARANLV AVVSNGTAVL GLGNIGPLAS KPVMEGKAVL FKKFAGIDVF 130 140 150 160 170 180 DIEIDAPTVD RMVDVISALE PTFGGINLED IKAPECFEVE RRLREKMEIP VFHDDQHGTA 190 200 210 220 230 240 IIVAAAVLNG LELAGKDIAE AKIVASGAGA AALACLNLLV TLGARRENIW VHDIEGLVYK 250 260 270 280 290 300 GREALMDEWK AVYAQESDNR VLADSIGGAD VFLGLSAAGV LKPELLARMA EKPLIMALAN 310 320 330 340 350 360 PTPEIMPEVA RAARPDAMIC TGRSDFPNQV NNVLCFPHIF RGALDCGART INEEMKMAAV 370 380 390 400 410 420 RAIAGLAREE PSDVAARAYS GETPVFGPDY LIPSPFDQRL ILRIAPAVAK AAAESGVATR 430 440 450 460 470 480 PIQDFDAYLD KLNRFVFRSG FIMKPVFAAA KNAAKNRVIF AEGEDERVLR AAQVLLEEGT 490 500 510 520 530 540 AKPILIGRPQ IIETRLRRYG LRIRPDVDFE VVNPEGDPRY RDYVDDYFAL VGRLGVIPEA 550 560 570 580 590 600 ARTIVRTNTT VIGALAVKRG EADALICGVE GRYSRHLRDV SQIIGKRSGV LDFSALSLLI 610 620 630 640 650 660 SQRGATFFTD TYVSFSPSAE EIAQTTVMAA NEIRRFGITP RAALVSHSNF GSRDSESAFK 670 680 690 700 710 720 MRTALQLVRE LAPDLEVDGE MHGDSAISEV LRQRVMPDST LNGEANLLVF PNLDAANITL 730 740 750 760 770 GVVKTMTDSL HVGPILLGSA LPAHILSPSV TSRGVVNMAA LAVVESSHPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes of Rhizobium (Sinorhizobium) meliloti." Mitsch M.J., Voegele R.T., Cowie A., Oesteras M., Finan T.M. J. Biol. Chem. 273:9330-9336(1998) [PubMed: 9535928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: RCR2011 / SU47.
[2]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[3]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[4]	"Characterization of two members of a novel malic enzyme class." Voegele R.T., Mitsch M.J., Finan T.M. Biochim. Biophys. Acta 1432:275-285(1999) [PubMed: 10407149] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF017443 Genomic DNA. Translation: AAB82459.1. AL591688 Genomic DNA. Translation: CAC46416.1.
RefSeq	NP_385943.1. NC_003047.1.
3D structure databases
ProteinModelPortal	O30807.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1233502.
GenomeReviews	Gene locus R01837 in contig AL591688_GR.
KEGG	sme:SMc00169.
NMPDR	fig|266834.1.peg.3131.
PATRIC	23633083. VBISinMel96828_3280.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289132.
OMA	RRENIWV.
ProtClustDB	PRK12862.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC00169-MONOMER.
Family and domain databases
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD-bd. IPR012188. ME_PTA. IPR016040. NAD(P)-bd_dom. IPR002505. PTA_PTB. [Graphical view]
Gene3D	G3DSA:3.40.50.10380. G3DSA:3.40.50.10380. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00028.
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. PF01515. PTA_PTB. 1 hit. [Graphical view]
PIRSF	PIRSF036684. ME_PTA. 1 hit.
SMART	SM00919. Malic_M. 1 hit. [Graphical view]
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAO1_RHIME

Accession

Primary (citable) accession number: O30807

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program