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Reviewed, UniProtKB/Swiss-Prot P27443 (MAOM_ASCSU)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NAD-dependent malic enzyme, mitochondrial
      Short name=NAD-ME
    EC=1.1.1.38
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

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Protein attributes

Sequence length643 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

(S)-malate + NAD+ = pyruvate + CO2 + NADH.

Cofactor

Divalent metal cations. Prefers magnesium or manganese.

Enzyme regulation

Subject to allosteric activation by fumarate.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix.

Miscellaneous

This isoenzyme can also use NADP+ but is more effective with NAD+.

Sequence similarities

Belongs to the malic enzymes family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 38›38Mitochondrion
Chain39 – 643605NAD-dependent malic enzyme, mitochondrial
PRO_0000018541

Regions

Nucleotide binding219 – 2279NAD
Nucleotide binding365 – 38218NAD

Sites

Active site1641Proton donor
Active site2371Proton acceptor
Metal binding3091Divalent metal cation
Metal binding3101Divalent metal cation
Metal binding3331Divalent metal cation Probable
Binding site781Allosteric activator
Binding site811Allosteric activator
Binding site1051Allosteric activator
Binding site3331NAD
Binding site4721NAD
Site3331Important for activity

Experimental info

Mutagenesis961E → A: Reduces activity over 1000-fold. Ref.2
Mutagenesis1641Y → F: Reduces activity over 60000-fold. Ref.3
Mutagenesis2161D → A: Reduces activity over 50-fold. Ref.2
Mutagenesis2371K → A: Reduces activity over 100000-fold. Ref.3
Mutagenesis2371K → R: Reduces activity over 10-fold. Ref.3
Mutagenesis3101D → A: Reduces activity over 800-fold. Ref.2
Mutagenesis3321D → A: Reduces activity over 13000-fold. Ref.2
Mutagenesis3331D → A: Reduces activity over 100000-fold. Ref.2
Mutagenesis3991D → A: Reduces activity 10-fold. Ref.2
Mutagenesis4781E → A: Reduces activity over 1000-fold. Ref.2
Non-terminal residue11

Secondary structure

1 ....................................................................................................... 643
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P27443-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 7B1A480F086FE267

FASTA64372,757
        10         20         30         40         50         60 
PRVRSFIAHQ SGITSVIRRS PDIAHRMVRS LSVSSQRNKS VAHHEDVYSH NLPPMDEKEM 

        70         80         90        100        110        120 
ALYKLYRPER VTPKKRSAEL LKEPRLNKGM GFSLYERQYL GLHGLLPPAF MTQEQQAYRV 

       130        140        150        160        170        180 
ITKLREQPND LARYIQLDGL QDRNEKLFYR VVCDHVKELM PIVYTPTVGL ACQNFGYIYR 

       190        200        210        220        230        240 
KPKGLYITIN DNSVSKIYQI LSNWHEEDVR AIVVTDGERI LGLGDLGAYG IGIPVGKLAL 

       250        260        270        280        290        300 
YVALGGVQPK WCLPVLLDVG TNNMDLLNDP FYIGLRHKRV RGKDYDTLLD NFMKACTKKY 

       310        320        330        340        350        360 
GQKTLIQFED FANPNAFRLL DKYQDKYTMF NDDIQGTASV IVAGLLTCTR VTKKLVSQEK 

       370        380        390        400        410        420 
YLFFGAGAAS TGIAEMIVHQ MQNEGISKEE ACNRIYLMDI DGLVTKNRKE MNPRHVQFAK 

       430        440        450        460        470        480 
DMPETTSILE VIRAARPGAL IGASTVRGAF NEEVIRAMAE INERPIIFAL SNPTSKAECT 

       490        500        510        520        530        540 
AEEAYTFTNG AALYASGSPF PNFELNGHTY KPGQGNNAYI FPGVALGTIL FQIRHVDNDL 

       550        560        570        580        590        600 
FLLAAKKVAS CVTEDSLKVG RVYPQLKEIR EISIQIAVEM AKYCYKNGTA NLYPQPEDLE 

       610        620        630        640 
KYVRAQVYNT EYEELINATY DWPEQDMRHG FPVPVVRHDS MDG

« Hide

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References

[1]"Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme."
Kulkarni G., Cook P.F., Harris B.G.
Arch. Biochem. Biophys. 300:231-237(1993) [PubMed: 8424657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis."
Karsten W.E., Chooback L., Liu D., Hwang C.-C., Lynch C., Cook P.F.
Biochemistry 38:10527-10532(1999) [PubMed: 10441149] [Abstract]
Cited for: MUTAGENESIS OF GLU-96; ASP-216; ASP-310; ASP-332; ASP-333; ASP-399 AND GLU-478.
[3]"Lysine 199 is the general acid in the NAD-malic enzyme reaction."
Liu D., Karsten W.E., Cook P.F.
Biochemistry 39:11955-11960(2000) [PubMed: 11009609] [Abstract]
Cited for: MUTAGENESIS OF TYR-164 AND LYS-237.
[4]"A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme."
Karsten W.E., Liu D., Rao G.S., Harris B.G., Cook P.F.
Biochemistry 44:3626-3635(2005) [PubMed: 15736972] [Abstract]
Cited for: MECHANISM, PH-DEPENDENCE OF ACTIVITY OF MUTANTS PHE-164; ARG-237 AND ALA-332.
[5]"Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution."
Coleman D.E., Rao G.S.J., Goldsmith E.J., Cook P.F., Harris B.G.
Biochemistry 41:6928-6938(2002) [PubMed: 12033925] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-643 IN COMPLEX WITH NAD.
[6]"Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site."
Rao G.S.J., Coleman D.E., Karsten W.E., Cook P.F., Harris B.G.
J. Biol. Chem. 278:38051-38058(2003) [PubMed: 12853453] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 39-643 IN COMPLEX WITH NAD; MAGNESIUM AND INHIBITOR.

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Cross-references

Sequence databases

M81055 mRNA. No translation available.
PIRS29742.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LLQX-ray2.30A/B39-643[»]
1O0SX-ray2.00A/B39-643[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.38. 649.

Family and domain databases

InterProIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N.
IPR012302. Malic_NAD_bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PRINTSPR00072. MALOXRDTASE.
PROSITEPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMAOM_ASCSU
AccessionPrimary (citable) accession number: P27443
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents