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Protein

NAD-dependent malic enzyme, mitochondrial

Gene

ME2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+, Mn2+Note: Divalent metal cations. Prefers magnesium or manganese.

Enzyme regulationi

Subject to allosteric activation by fumarate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671Allosteric activator2 Publications
Binding sitei91 – 911Allosteric activator2 Publications
Active sitei112 – 1121Proton donor
Binding sitei165 – 1651Substrate1 Publication
Active sitei183 – 1831Proton acceptor
Metal bindingi255 – 2551Divalent metal cation
Metal bindingi256 – 2561Divalent metal cation
Binding sitei259 – 2591NAD2 Publications
Metal bindingi279 – 2791Divalent metal cation
Sitei279 – 2791Important for activityBy similarity
Binding sitei421 – 4211Substrate1 Publication
Binding sitei466 – 4661Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1739NAD2 Publications
Nucleotide bindingi311 – 32818NAD2 PublicationsAdd
BLAST

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. malate dehydrogenase (decarboxylating) (NAD+) activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. oxaloacetate decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. malate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD

Enzyme and pathway databases

SABIO-RKP23368.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent malic enzyme, mitochondrial (EC:1.1.1.38)
Short name:
NAD-ME
Alternative name(s):
Malic enzyme 2
Gene namesi
Name:ME2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6984. ME2.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671R → S: Abolishes activation by fumarate. 1 Publication
Mutagenesisi91 – 911R → T: Abolishes activation by fumarate. 1 Publication

Organism-specific databases

PharmGKBiPA30724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818Mitochondrion1 PublicationAdd
BLAST
Chaini19 – 584566NAD-dependent malic enzyme, mitochondrialPRO_0000018537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561N6-acetyllysine1 Publication
Modified residuei224 – 2241N6-acetyllysine1 Publication
Modified residuei240 – 2401N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP23368.
PaxDbiP23368.
PeptideAtlasiP23368.
PRIDEiP23368.

PTM databases

PhosphoSiteiP23368.

Expressioni

Gene expression databases

BgeeiP23368.
CleanExiHS_ME2.
GenevestigatoriP23368.

Organism-specific databases

HPAiHPA008247.
HPA008880.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

BioGridi110364. 3 interactions.
IntActiP23368. 1 interaction.
MINTiMINT-4530114.
STRINGi9606.ENSP00000321070.

Structurei

Secondary structure

1
584
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304Combined sources
Turni32 – 343Combined sources
Helixi37 – 393Combined sources
Helixi42 – 476Combined sources
Turni51 – 533Combined sources
Helixi61 – 7414Combined sources
Helixi78 – 8912Combined sources
Helixi93 – 10210Combined sources
Helixi104 – 1118Combined sources
Helixi115 – 1217Combined sources
Helixi123 – 1264Combined sources
Beta strandi132 – 1365Combined sources
Helixi137 – 1393Combined sources
Turni140 – 1423Combined sources
Helixi143 – 1475Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi163 – 1653Combined sources
Turni167 – 1693Combined sources
Helixi173 – 1775Combined sources
Helixi178 – 19114Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2058Combined sources
Helixi212 – 2143Combined sources
Helixi229 – 24618Combined sources
Beta strandi251 – 2544Combined sources
Helixi259 – 26911Combined sources
Turni270 – 2723Combined sources
Beta strandi273 – 2775Combined sources
Helixi278 – 29821Combined sources
Helixi302 – 3043Combined sources
Beta strandi307 – 3104Combined sources
Helixi314 – 32916Combined sources
Helixi334 – 3396Combined sources
Beta strandi341 – 3455Combined sources
Turni360 – 3623Combined sources
Helixi363 – 3653Combined sources
Helixi377 – 3848Combined sources
Beta strandi387 – 3915Combined sources
Beta strandi394 – 3963Combined sources
Helixi401 – 41010Combined sources
Beta strandi415 – 4184Combined sources
Helixi423 – 4253Combined sources
Beta strandi426 – 4283Combined sources
Helixi430 – 4367Combined sources
Turni437 – 4393Combined sources
Beta strandi442 – 4476Combined sources
Helixi467 – 4693Combined sources
Helixi471 – 48010Combined sources
Helixi488 – 49912Combined sources
Helixi504 – 5085Combined sources
Helixi516 – 5183Combined sources
Helixi519 – 53618Combined sources
Helixi549 – 5557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DO8X-ray2.20A/B/C/D21-584[»]
1EFKX-ray2.60A/B/C/D1-584[»]
1EFLX-ray2.60A/B/C/D1-584[»]
1GZ3X-ray2.30A/B/C/D20-573[»]
1GZ4X-ray2.20A/B/C/D23-573[»]
1PJ2X-ray2.30A/B/C/D21-584[»]
1PJ3X-ray2.10A/B/C/D21-584[»]
1PJ4X-ray2.30A/B/C/D21-584[»]
1PJLX-ray2.90A/B/C/D/E/F/G/H1-584[»]
1QR6X-ray2.10A/B1-584[»]
ProteinModelPortaliP23368.
SMRiP23368. Positions 21-573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23368.

Family & Domainsi

Sequence similaritiesi

Belongs to the malic enzymes family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0281.
GeneTreeiENSGT00390000000754.
HOGENOMiHOG000042486.
HOVERGENiHBG000746.
InParanoidiP23368.
KOiK00027.
OMAiKAKYIRE.
OrthoDBiEOG7G4QF0.
PhylomeDBiP23368.
TreeFamiTF300537.

Family and domain databases

Gene3Di3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PIRSFiPIRSF000106. ME. 1 hit.
PRINTSiPR00072. MALOXRDTASE.
SMARTiSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23368-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRLRVVST TCTLACRHLH IKEKGKPLML NPRTNKGMAF TLQERQMLGL
60 70 80 90 100
QGLLPPKIET QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL
110 120 130 140 150
QDDIESLMPI VYTPTVGLAC SQYGHIFRRP KGLFISISDR GHVRSIVDNW
160 170 180 190 200
PENHVKAVVV TDGERILGLG DLGVYGMGIP VGKLCLYTAC AGIRPDRCLP
210 220 230 240 250
VCIDVGTDNI ALLKDPFYMG LYQKRDRTQQ YDDLIDEFMK AITDRYGRNT
260 270 280 290 300
LIQFEDFGNH NAFRFLRKYR EKYCTFNDDI QGTAAVALAG LLAAQKVISK
310 320 330 340 350
PISEHKILFL GAGEAALGIA NLIVMSMVEN GLSEQEAQKK IWMFDKYGLL
360 370 380 390 400
VKGRKAKIDS YQEPFTHSAP ESIPDTFEDA VNILKPSTII GVAGAGRLFT
410 420 430 440 450
PDVIRAMASI NERPVIFALS NPTAQAECTA EEAYTLTEGR CLFASGSPFG
460 470 480 490 500
PVKLTDGRVF TPGQGNNVYI FPGVALAVIL CNTRHISDSV FLEAAKALTS
510 520 530 540 550
QLTDEELAQG RLYPPLANIQ EVSINIAIKV TEYLYANKMA FRYPEPEDKA
560 570 580
KYVKERTWRS EYDSLLPDVY EWPESASSPP VITE
Length:584
Mass (Da):65,444
Last modified:November 1, 1991 - v1
Checksum:i4CEF9AF89B07D93D
GO
Isoform 2 (identifier: P23368-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-584: VALAVILCNT...SASSPPVITE → YRIPIC

Note: No experimental confirmation available.

Show »
Length:479
Mass (Da):53,586
Checksum:i8F4D1C728EDD83E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti263 – 2631F → Y in BAG36189. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141P → L.
Corresponds to variant rs16952692 [ dbSNP | Ensembl ].
VAR_034104
Natural varianti450 – 4501G → E.
Corresponds to variant rs649224 [ dbSNP | Ensembl ].
VAR_050017

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei474 – 584111VALAV…PVITE → YRIPIC in isoform 2. 1 PublicationVSP_042717Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55905 mRNA. Translation: AAA36197.1.
AB045122 Genomic DNA. Translation: BAB40980.1.
AK313391 mRNA. Translation: BAG36189.1.
AC015864 Genomic DNA. No translation available.
AC087687 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62980.1.
BC000147 mRNA. Translation: AAH00147.1.
AJ294818 mRNA. Translation: CAC14574.1.
CCDSiCCDS11948.1. [P23368-1]
CCDS54187.1. [P23368-2]
PIRiA39503.
RefSeqiNP_001161807.1. NM_001168335.1. [P23368-2]
NP_002387.1. NM_002396.4. [P23368-1]
UniGeneiHs.233119.

Genome annotation databases

EnsembliENST00000321341; ENSP00000321070; ENSG00000082212. [P23368-1]
ENST00000382927; ENSP00000372384; ENSG00000082212. [P23368-2]
GeneIDi4200.
KEGGihsa:4200.
UCSCiuc002ley.3. human. [P23368-1]
uc010dpd.3. human. [P23368-2]

Polymorphism databases

DMDMi126733.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55905 mRNA. Translation: AAA36197.1.
AB045122 Genomic DNA. Translation: BAB40980.1.
AK313391 mRNA. Translation: BAG36189.1.
AC015864 Genomic DNA. No translation available.
AC087687 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62980.1.
BC000147 mRNA. Translation: AAH00147.1.
AJ294818 mRNA. Translation: CAC14574.1.
CCDSiCCDS11948.1. [P23368-1]
CCDS54187.1. [P23368-2]
PIRiA39503.
RefSeqiNP_001161807.1. NM_001168335.1. [P23368-2]
NP_002387.1. NM_002396.4. [P23368-1]
UniGeneiHs.233119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DO8X-ray2.20A/B/C/D21-584[»]
1EFKX-ray2.60A/B/C/D1-584[»]
1EFLX-ray2.60A/B/C/D1-584[»]
1GZ3X-ray2.30A/B/C/D20-573[»]
1GZ4X-ray2.20A/B/C/D23-573[»]
1PJ2X-ray2.30A/B/C/D21-584[»]
1PJ3X-ray2.10A/B/C/D21-584[»]
1PJ4X-ray2.30A/B/C/D21-584[»]
1PJLX-ray2.90A/B/C/D/E/F/G/H1-584[»]
1QR6X-ray2.10A/B1-584[»]
ProteinModelPortaliP23368.
SMRiP23368. Positions 21-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110364. 3 interactions.
IntActiP23368. 1 interaction.
MINTiMINT-4530114.
STRINGi9606.ENSP00000321070.

PTM databases

PhosphoSiteiP23368.

Polymorphism databases

DMDMi126733.

Proteomic databases

MaxQBiP23368.
PaxDbiP23368.
PeptideAtlasiP23368.
PRIDEiP23368.

Protocols and materials databases

DNASUi4200.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321341; ENSP00000321070; ENSG00000082212. [P23368-1]
ENST00000382927; ENSP00000372384; ENSG00000082212. [P23368-2]
GeneIDi4200.
KEGGihsa:4200.
UCSCiuc002ley.3. human. [P23368-1]
uc010dpd.3. human. [P23368-2]

Organism-specific databases

CTDi4200.
GeneCardsiGC18P048405.
HGNCiHGNC:6984. ME2.
HPAiHPA008247.
HPA008880.
MIMi154270. gene.
neXtProtiNX_P23368.
PharmGKBiPA30724.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0281.
GeneTreeiENSGT00390000000754.
HOGENOMiHOG000042486.
HOVERGENiHBG000746.
InParanoidiP23368.
KOiK00027.
OMAiKAKYIRE.
OrthoDBiEOG7G4QF0.
PhylomeDBiP23368.
TreeFamiTF300537.

Enzyme and pathway databases

SABIO-RKP23368.

Miscellaneous databases

EvolutionaryTraceiP23368.
GeneWikiiME2.
ME2_(gene).
GenomeRNAii4200.
NextBioi16554.
PROiP23368.
SOURCEiSearch...

Gene expression databases

BgeeiP23368.
CleanExiHS_ME2.
GenevestigatoriP23368.

Family and domain databases

Gene3Di3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PIRSFiPIRSF000106. ME. 1 hit.
PRINTSiPR00072. MALOXRDTASE.
SMARTiSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli."
    Loeber G., Infante A.A., Maurer-Fogy I., Krystek E., Dworkin M.B.
    J. Biol. Chem. 266:3016-3021(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "Physical and transcriptional map of a 311-kb segment of chromosome 18q21, a candidate lung tumor suppressor locus."
    Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N., Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y., Hagiwara K., Tanaka T., Yokota J.
    Genomics 72:169-179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-80.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Trachea.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  7. Abts H.
    Thesis (1995), University of Cologne, Germany
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 421-584 (ISOFORM 1).
    Tissue: B-cell.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-33.
    Tissue: Platelet.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156; LYS-224; LYS-240; LYS-272 AND LYS-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases."
    Xu Y., Bhargava G., Wu H., Loeber G., Tong L.
    Structure 7:877-889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  12. "Structure of a closed form of human malic enzyme and implications for catalytic mechanism."
    Yang Z., Floyd D.L., Loeber G., Tong L.
    Nat. Struct. Biol. 7:251-257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-584 IN COMPLEX WITH NAD; DIVALENT METAL ION AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
  13. "Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate."
    Yang Z., Lanks C.W., Tong L.
    Structure 10:951-960(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-573 IN COMPLEX WITH ATP; MANGANESE; ALLOSTERIC ACTIVATOR AND SUBSTRATE ANALOG, MUTAGENESIS OF ARG-67 AND ARG-91, HOMOTETRAMERIZATION.
  14. "Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism."
    Tao X., Yang Z., Tong L.
    Structure 11:1141-1150(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-584 IN COMPLEX WITH SUBSTRATE; NAD; MANGANESE AND ALLOSTERIC ACTIVATOR, ENZYME MECHANISM.

Entry informationi

Entry nameiMAOM_HUMAN
AccessioniPrimary (citable) accession number: P23368
Secondary accession number(s): B2R8J2
, Q9BWL6, Q9BYG1, Q9H4B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 7, 2015
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.