Q5QWY8 (MAO1_IDILO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD-dependent malic enzyme
Short name=NAD-ME
EC=1.1.1.38

Gene names

Name:	maeA
Ordered Locus Names:	IL0598

Organism

Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]

Taxonomic identifier

283942 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-malate + NAD+ = pyruvate + CO2 + NADH. HAMAP MF_01619
Cofactor	Divalent metal cations. Prefers magnesium or manganese By similarity.
Subunit structure	Homotetramer By similarity. HAMAP MF_01619
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Ligand	Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	NAD 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 – 562	562	NAD-dependent malic enzyme HAMAP MF_01619		PRO_0000160219
Sites
	Active site	101	1	Proton donor By similarity
	Active site	172	1	Proton acceptor By similarity
	Metal binding	243	1	Divalent metal cation By similarity
	Metal binding	244	1	Divalent metal cation By similarity
	Metal binding	267	1	Divalent metal cation By similarity
	Binding site	154	1	NAD By similarity
	Binding site	267	1	NAD By similarity
	Binding site	415	1	NAD By similarity
	Site	267	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5QWY8 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 2BD4C66FC61FFCB2	FASTA	562	62,784
	10 20 30 40 50 60 MPQTQRPLYI PYSGPNLLET PLLNKGSAFS KEERAAFNLT GLLPPRYESI EEQAERAYMQ 70 80 90 100 110 120 YRSFETPINK HIYLRAIQDN NETLFYRLLT DHLEEMMPII YTPTVGDACE KFSDIYRSSR 130 140 150 160 170 180 GLFISYSERD QIDDILRNAT KQKVKVIVVT DGERILGLGD QGIGGMGIPI GKLSLYTACG 190 200 210 220 230 240 GISPAYTLPV MLDVGTNNEK LLEDPMYMGA RHKRIEQDEY DEFLDKFIKA VTRRWPGVML 250 260 270 280 290 300 QFEDFAQPNA MPLLRRYRDE VCCFNDDIQG TASVTVGTLL AACRQKGKKL SEQKVVFVGA 310 320 330 340 350 360 GSAGCGIAEQ IMIQMTAEGL TEEQAKRQIF MVDRFGLVMD TMDGLRDFQQ ALAQKTSDLN 370 380 390 400 410 420 AWEYSGEYPS LLDVMHCAEP DILIGVSGQA GLFTEQVIST MAKNVERPII FPLSNPSKHV 430 440 450 460 470 480 EAHPADVLKW SEGKAIVATG SPFGEVEYDG RIYPIAQCNN SYIFPGIGLG VLSVKSERVS 490 500 510 520 530 540 DEMLRVASKT LANASPSANG KGEALLPAFN DLTQLSKDIA FAVGKVAQQE GLALEIDDDT 550 560 LRERIDNNFW KPEYRFYKRV SI

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV81439.1.
RefSeq	YP_154988.1. NC_006512.1.
3D structure databases
ProteinModelPortal	Q5QWY8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3174600.
GenomeReviews	Gene locus IL0598 in contig AE017340_GR.
KEGG	ilo:IL0598.
NMPDR	fig|283942.3.peg.977.
PATRIC	22139217. VBIIdiLoi21852_0600.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289821.
OMA	QDNNETL.
ProtClustDB	PRK13529.
Enzyme and pathway databases
BioCyc	ILOI283942:IL0598-MONOMER.
Family and domain databases
HAMAP	MF_01619. NAD_malic_enz. [Tree]
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD-bd. IPR001891. Malic_OxRdtase. IPR016040. NAD(P)-bd_dom. IPR023667. NAD_malic_enz_proteobac. [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	K00027.
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PIRSF	PIRSF000106. ME. 1 hit.
PRINTS	PR00072. MALOXRDTASE.
SMART	SM00919. Malic_M. 1 hit. [Graphical view]
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAO1_IDILO

Accession

Primary (citable) accession number: Q5QWY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program