Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADP-dependent malic enzyme

Gene

tme

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NADP+ = pyruvate + CO2 + NADPH.
Oxaloacetate = pyruvate + CO2.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton donorBy similarity
Metal bindingi146 – 1461Divalent metal cationBy similarity
Metal bindingi147 – 1471Divalent metal cationBy similarity
Active sitei172 – 1721Proton acceptorBy similarity
Binding sitei172 – 1721NADBy similarity
Binding sitei297 – 2971NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NADP

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-396-MONOMER.
SMEL266834:GJF6-405-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent malic enzyme (EC:1.1.1.40)
Short name:
NADP-ME
Gene namesi
Name:tme
Ordered Locus Names:R00394
ORF Names:SMc01126
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
Proteomesi
  • UP000001976 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 761761NADP-dependent malic enzymePRO_0000160246Add
BLAST

Proteomic databases

PRIDEiO30808.

Interactioni

Subunit structurei

Homooctamer.

Protein-protein interaction databases

STRINGi266834.SMc01126.

Structurei

3D structure databases

ProteinModelPortaliO30808.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 437437Malic enzymeAdd
BLAST
Regioni438 – 761324Phosphate acetyltransferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the malic enzymes family.Curated
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

Phylogenomic databases

eggNOGiENOG4105C6K. Bacteria.
COG0280. LUCA.
COG0281. LUCA.
HOGENOMiHOG000132448.
KOiK00029.
OMAiGYLYRDC.
OrthoDBiEOG6QCD9W.

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.
IPR012188. ME_PTA.
IPR016040. NAD(P)-bd_dom.
IPR002505. PTA_PTB.
[Graphical view]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFiPIRSF036684. ME_PTA. 1 hit.
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: Complete.

O30808-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGIDKTDRA MTSVTAQEAL DFHSQGRPGK LEISPTKPMA TQRDLSLAYS
60 70 80 90 100
PGVAVPVKAI ADDPATAYDY TARGNMVAVI SNGTAILGLG NLGALASKPV
110 120 130 140 150
MEGKAVLFKR FADVDSIDLE VDTENVDEFV NCVRFLGPSF GGINLEDIKA
160 170 180 190 200
PDCFIIEQRL REVMDIPVFH DDQHGTAIIA AAGLVNALTL TGRDFKTAKL
210 220 230 240 250
VCNGAGAAAI ACIELIKAMG FNPENIILCD TKGVIYKGRT DGMNQWKSAH
260 270 280 290 300
AVETDRRTLA EALDGADVFF GLSAKGALSA DMVRSMGARP IIFAMANPDP
310 320 330 340 350
EITPEEVALI RDDAIVATGR SDYPNQVNNV LGFPYIFRGA LDVRASTIND
360 370 380 390 400
AMKIAAAEAL ANLAKEDVPD DVAAAYQGNR PRFGPQYIIP VPFDPRLISA
410 420 430 440 450
IPMAVAKAAM ETGVARKPIE DLKAYGQQLS ARRDPIASTL QRIVERVRRQ
460 470 480 490 500
PKRIVFAEGE EVQMMRSAIA YANQQLGTAL LLGREEVMRE TAEREGIDLD
510 520 530 540 550
RAGIQIVNAR LSKRVGAYTD FLYSRLQRKG YLFRDVQRLI NTDRNHFAAS
560 570 580 590 600
MVALGDADGM VTGLTRNYST ALEDVRRCID PKPGHRVIGV SIALCRGRTV
610 620 630 640 650
LVADTAVHDM PTSEELADIA EEAAGLAKRL GYVPRVAMLA YSTFGHPSGE
660 670 680 690 700
RSERVREAVK ILDRRRVDFE YDGEMAADVA LNARVMEQYP FCRLSGTANV
710 720 730 740 750
LVMPAFHSAS ISTKMLQELG GSTVIGPLLV GLDKSVQIAS MSAKDSDLVN
760
LAAIAAYNAG T
Length:761
Mass (Da):82,209
Last modified:May 30, 2000 - v2
Checksum:iA342A5F41F39DBC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281L → F in AAB82460 (PubMed:9535928).Curated
Sequence conflicti609 – 63628DMPTS…YVPRV → KHADLRGAG in AAB82460 (PubMed:9535928).CuratedAdd
BLAST
Sequence conflicti761 – 7611T → TRRGSAESRKTAGTSSVAAS PDG in AAB82460 (PubMed:9535928).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017444 Genomic DNA. Translation: AAB82460.1.
AL591688 Genomic DNA. Translation: CAC41831.1.
RefSeqiNP_384500.1. NC_003047.1.
WP_010968547.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC41831; CAC41831; SMc01126.
GeneIDi1232028.
KEGGisme:SMc01126.
PATRICi23629995. VBISinMel96828_1767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017444 Genomic DNA. Translation: AAB82460.1.
AL591688 Genomic DNA. Translation: CAC41831.1.
RefSeqiNP_384500.1. NC_003047.1.
WP_010968547.1. NC_003047.1.

3D structure databases

ProteinModelPortaliO30808.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266834.SMc01126.

Proteomic databases

PRIDEiO30808.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC41831; CAC41831; SMc01126.
GeneIDi1232028.
KEGGisme:SMc01126.
PATRICi23629995. VBISinMel96828_1767.

Phylogenomic databases

eggNOGiENOG4105C6K. Bacteria.
COG0280. LUCA.
COG0281. LUCA.
HOGENOMiHOG000132448.
KOiK00029.
OMAiGYLYRDC.
OrthoDBiEOG6QCD9W.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-396-MONOMER.
SMEL266834:GJF6-405-MONOMER.

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.
IPR012188. ME_PTA.
IPR016040. NAD(P)-bd_dom.
IPR002505. PTA_PTB.
[Graphical view]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFiPIRSF036684. ME_PTA. 1 hit.
SMARTiSM01274. malic. 1 hit.
SM00919. Malic_M. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes of Rhizobium (Sinorhizobium) meliloti."
    Mitsch M.J., Voegele R.T., Cowie A., Oesteras M., Finan T.M.
    J. Biol. Chem. 273:9330-9336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: RCR2011 / SU47.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  4. "Characterization of two members of a novel malic enzyme class."
    Voegele R.T., Mitsch M.J., Finan T.M.
    Biochim. Biophys. Acta 1432:275-285(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiMAO2_RHIME
AccessioniPrimary (citable) accession number: O30808
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. 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.