Reviewed, UniProtKB/Swiss-Prot P78715 (MAOH_NEOFR)

Names and origin

Protein names	Recommended name:     Malic enzyme, hydrogenosomal       Short name=ME     EC=1.1.1.40
Organism	Neocallimastix frontalis (Rumen fungus)
Taxonomic identifier	4757 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Neocallimastigomycota › Neocallimastigomycetes › Neocallimastigales › Neocallimastigaceae › Neocallimastix

Protein attributes

Sequence length	592 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 + NADP+ = pyruvate + CO2 + NADPH.
Cofactor	Divalent metal cations. Prefers magnesium or manganese By similarity.
Subcellular location	Hydrogenosome.
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Cellular component	Hydrogenosome
Domain	Transit peptide
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	hydrogenosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) 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
	Transit peptide	1 – 27	27	Hydrogenosome
	Chain	28 – 592	565	Malic enzyme, hydrogenosomal		PRO_0000018549
Regions
	Nucleotide binding	182 – 205	24	NADP By similarity
	Nucleotide binding	335 – 352	18	NADP By similarity
Sites
	Active site	134	1	Proton donor By similarity
	Active site	205	1	Proton acceptor By similarity
	Metal binding	276	1	Divalent metal cation By similarity
	Metal binding	277	1	Divalent metal cation By similarity
	Metal binding	300	1	Divalent metal cation By similarity
	Binding site	187	1	NAD By similarity
	Binding site	300	1	NAD By similarity
	Binding site	443	1	NAD By similarity
	Site	300	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P78715-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 5BB891C4FDA127BF	FASTA	592	65,546
	10 20 30 40 50 60 MLAPIQTIAR PVSSILPATG ALAAKRTFFA PSEVYNKKQV IVTKKTGLDI LNDPKLNKGS 70 80 90 100 110 120 AFTADEKDRL GIRGLVPPRP QSLEAQYKRC KTNLDKISDP LEKFIYLNHL QNRNETLYYK 130 140 150 160 170 180 MILENFVELA PIIYTPVVGE ACQKFHKIFT QTRGMYFSTA DRGQMSAVAA NWPYDDVDVI 190 200 210 220 230 240 VVTDGSRILG LGDLGAGGMQ IPIGKLTLYV CGGGINPRNV LPIVLDVGTN NKELLNDPLY 250 260 270 280 290 300 LGMQHPRLQG EEFHAFVDEW VSAITDRFPK AVIQFEDFMM PNALDLLLKY KDQICMFNDD 310 320 330 340 350 360 IQSTGAITLA SVLATMRARG GTFADIKKET FLCLGAGSSG VGVCETIVDC IVAEGATREE 370 380 390 400 410 420 AYAQFYMFDH KGLLGKGRDD LLPSQQVFMR KEIEGGKTPA ELLKKIKPTC LLGLSTCPKL 430 440 450 460 470 480 FNKEMLSYVA SYCEKPGIFP LSNPTSRSEC TAEEAVEFTD GNLIFASGSP FDPVEWKGKT 490 500 510 520 530 540 IQTNQCNNSY SFPGIGLGLV SSRATRVPFE TFQVCARVIA SLGTPEMLAT GKIFPDLDNL 550 560 570 580 590 RAVSLEVGIE VAKMAERMNI ATQFPPKGMD WREWLKHNMW QPEYPHIVVK NL

References

[1]

"A mitochondrial-like targeting signal on the hydrogenosomal malic enzyme from the anaerobic fungus Neocallimastix frontalis: support for the hypothesis that hydrogenosomes are modified mitochondria." van der Giezen M., Rechinger K.B., Svendsen I., Durand R., Hirt R.P., Fevre M., Embley T.M., Prins R.A. Mol. Microbiol. 23:11-21(1997) [PubMed: 9004216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: L2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U62041 mRNA. Translation: AAC49572.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQ2 based on UniProtKB P40927.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.40. 448.
Family and domain databases
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR001891. Malic_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PRINTS	PR00072. MALOXRDTASE.
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAOH_NEOFR

Accession

Primary (citable) accession number: P78715

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)