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Protein

NAD-dependent malic enzyme, mitochondrial

Gene
N/A
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
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)DescriptionActionsGraphical viewLength
Binding sitei78Allosteric activator1
Binding sitei81Allosteric activator1
Binding sitei105Allosteric activator1
Active sitei164Proton donor1
Active sitei237Proton acceptor1
Metal bindingi309Divalent metal cation1
Metal bindingi310Divalent metal cation1
Metal bindingi333Divalent metal cationCurated1
Binding sitei333NAD2 Publications1
Sitei333Important for activity1
Binding sitei472NAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi219 – 227NAD2 Publications9
Nucleotide bindingi365 – 382NAD2 PublicationsAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18298.
BRENDAi1.1.1.38. 474.
SABIO-RKP27443.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent malic enzyme, mitochondrial (EC:1.1.1.38)
Short name:
NAD-ME
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96E → A: Reduces activity over 1000-fold. 1 Publication1
Mutagenesisi164Y → F: Reduces activity over 60000-fold. 1 Publication1
Mutagenesisi216D → A: Reduces activity over 50-fold. 1 Publication1
Mutagenesisi237K → A: Reduces activity over 100000-fold. 1 Publication1
Mutagenesisi237K → R: Reduces activity over 10-fold. 1 Publication1
Mutagenesisi310D → A: Reduces activity over 800-fold. 1 Publication1
Mutagenesisi332D → A: Reduces activity over 13000-fold. 1 Publication1
Mutagenesisi333D → A: Reduces activity over 100000-fold. 1 Publication1
Mutagenesisi399D → A: Reduces activity 10-fold. 1 Publication1
Mutagenesisi478E → A: Reduces activity over 1000-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 38MitochondrionAdd BLAST›38
ChainiPRO_000001854139 – 643NAD-dependent malic enzyme, mitochondrialAdd BLAST605

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi57 – 66Combined sources10
Helixi77 – 81Combined sources5
Turni84 – 86Combined sources3
Helixi89 – 91Combined sources3
Helixi94 – 99Combined sources6
Turni103 – 105Combined sources3
Helixi113 – 126Combined sources14
Beta strandi127 – 129Combined sources3
Helixi130 – 143Combined sources14
Helixi145 – 154Combined sources10
Helixi156 – 163Combined sources8
Helixi167 – 175Combined sources9
Beta strandi184 – 188Combined sources5
Helixi189 – 191Combined sources3
Helixi194 – 201Combined sources8
Beta strandi211 – 215Combined sources5
Beta strandi217 – 220Combined sources4
Turni221 – 223Combined sources3
Helixi227 – 231Combined sources5
Helixi232 – 245Combined sources14
Helixi249 – 251Combined sources3
Beta strandi252 – 259Combined sources8
Helixi264 – 268Combined sources5
Helixi283 – 300Combined sources18
Beta strandi305 – 308Combined sources4
Helixi313 – 323Combined sources11
Turni324 – 326Combined sources3
Beta strandi327 – 331Combined sources5
Helixi332 – 352Combined sources21
Helixi356 – 358Combined sources3
Beta strandi361 – 364Combined sources4
Helixi368 – 382Combined sources15
Turni383 – 385Combined sources3
Helixi388 – 393Combined sources6
Beta strandi395 – 399Combined sources5
Beta strandi405 – 407Combined sources3
Helixi413 – 415Combined sources3
Turni416 – 418Combined sources3
Beta strandi420 – 422Combined sources3
Helixi428 – 435Combined sources8
Beta strandi438 – 442Combined sources5
Helixi452 – 461Combined sources10
Beta strandi466 – 469Combined sources4
Helixi474 – 476Combined sources3
Helixi481 – 486Combined sources6
Turni487 – 489Combined sources3
Beta strandi493 – 498Combined sources6
Beta strandi503 – 505Combined sources3
Beta strandi508 – 510Combined sources3
Helixi517 – 519Combined sources3
Helixi521 – 531Combined sources11
Helixi538 – 550Combined sources13
Helixi554 – 557Combined sources4
Turni558 – 560Combined sources3
Helixi566 – 568Combined sources3
Helixi569 – 586Combined sources18
Beta strandi592 – 594Combined sources3
Helixi599 – 606Combined sources8
Helixi624 – 627Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLQX-ray2.30A/B39-643[»]
1O0SX-ray2.00A/B39-643[»]
ProteinModelPortaliP27443.
SMRiP27443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27443.

Family & Domainsi

Sequence similaritiesi

Belongs to the malic enzymes family.Curated

Keywords - Domaini

Transit peptide

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.
SMARTiSM01274. malic. 1 hit.
SM00919. Malic_M. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P27443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PRVRSFIAHQ SGITSVIRRS PDIAHRMVRS LSVSSQRNKS VAHHEDVYSH
60 70 80 90 100
NLPPMDEKEM ALYKLYRPER VTPKKRSAEL LKEPRLNKGM GFSLYERQYL
110 120 130 140 150
GLHGLLPPAF MTQEQQAYRV ITKLREQPND LARYIQLDGL QDRNEKLFYR
160 170 180 190 200
VVCDHVKELM PIVYTPTVGL ACQNFGYIYR KPKGLYITIN DNSVSKIYQI
210 220 230 240 250
LSNWHEEDVR AIVVTDGERI LGLGDLGAYG IGIPVGKLAL YVALGGVQPK
260 270 280 290 300
WCLPVLLDVG TNNMDLLNDP FYIGLRHKRV RGKDYDTLLD NFMKACTKKY
310 320 330 340 350
GQKTLIQFED FANPNAFRLL DKYQDKYTMF NDDIQGTASV IVAGLLTCTR
360 370 380 390 400
VTKKLVSQEK YLFFGAGAAS TGIAEMIVHQ MQNEGISKEE ACNRIYLMDI
410 420 430 440 450
DGLVTKNRKE MNPRHVQFAK DMPETTSILE VIRAARPGAL IGASTVRGAF
460 470 480 490 500
NEEVIRAMAE INERPIIFAL SNPTSKAECT AEEAYTFTNG AALYASGSPF
510 520 530 540 550
PNFELNGHTY KPGQGNNAYI FPGVALGTIL FQIRHVDNDL FLLAAKKVAS
560 570 580 590 600
CVTEDSLKVG RVYPQLKEIR EISIQIAVEM AKYCYKNGTA NLYPQPEDLE
610 620 630 640
KYVRAQVYNT EYEELINATY DWPEQDMRHG FPVPVVRHDS MDG
Length:643
Mass (Da):72,757
Last modified:August 1, 1992 - v1
Checksum:i7B1A480F086FE267
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81055 mRNA. No translation available.
PIRiS29742.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81055 mRNA. No translation available.
PIRiS29742.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLQX-ray2.30A/B39-643[»]
1O0SX-ray2.00A/B39-643[»]
ProteinModelPortaliP27443.
SMRiP27443.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18298.
BRENDAi1.1.1.38. 474.
SABIO-RKP27443.

Miscellaneous databases

EvolutionaryTraceiP27443.

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.
SMARTiSM01274. malic. 1 hit.
SM00919. Malic_M. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAOM_ASCSU
AccessioniPrimary (citable) accession number: P27443
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Allosteric enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.