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Protein

Bifunctional protein MdtA

Gene

mtdA

Organism
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydrogenation of methylene-H4MPT. Can also catalyze the reversible dehydrogenation of methylene-H4F with 20-fold lower catalytic efficiency.1 Publication

Catalytic activityi

5,10-methylenetetrahydromethanopterin + NADP+ = 5,10-methenyltetrahydromethanopterin + NADPH.1 Publication
5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.2 Publications

Kineticsi

  1. KM=20 mM for methylenetetrahydromethanopterin1 Publication
  2. KM=30 mM for methylenetetrahydrofolate1 Publication
  3. KM=30 mM for NADP+ (in the presence of methylenetetrahydromethanopterin)1 Publication
  4. KM=10 mM for NADP+ (in the presence of methylenetetrahydrofolate)1 Publication
  1. Vmax=600 µmol/min/mg enzyme with methylenetetrahydromethanopterin as substrate1 Publication
  2. Vmax=30 µmol/min/mg enzyme with methylenetetrahydrofolate as substrate1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

Pathwayi: formaldehyde degradation

This protein is involved in step 2 of the subpathway that synthesizes formate from formaldehyde (H(4)MPT route).1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. 5,6,7,8-tetrahydromethanopterin hydro-lyase (fae)
  2. Bifunctional protein MdtA (mtdA), NAD(P)-dependent methylenetetrahydromethanopterin dehydrogenase (mtdB)
  3. Methenyltetrahydromethanopterin cyclohydrolase (mch)
  4. Formyltransferase/hydrolase complex Fhc subunit B (fhcB), Formyltransferase/hydrolase complex Fhc subunit A (fhcA), Formyltransferase/hydrolase complex subunit D (fhcD), Formyltransferase/hydrolase complex Fhc subunit C (fhcC)
  5. no protein annotated in this organism
This subpathway is part of the pathway formaldehyde degradation, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formate from formaldehyde (H(4)MPT route), the pathway formaldehyde degradation and in One-carbon metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei256NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi129 – 132NADP1 Publication4
Nucleotide bindingi152 – 156NADP1 Publication5
Nucleotide bindingi195 – 198NADP1 Publication4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processOne-carbon metabolism
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3941.
UniPathwayiUPA00562; UER00702.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein MdtACurated
Including the following 2 domains:
NADP-dependent methylenetetrahydromethanopterin dehydrogenase1 Publication (EC:1.5.1.-1 Publication)
Methylenetetrahydrofolate dehydrogenase1 Publication (EC:1.5.1.52 Publications)
Gene namesi
Name:mtdA1 Publication
Ordered Locus Names:MexAM1_META1p1728
OrganismiMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
Taxonomic identifieri272630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
Proteomesi
  • UP000009081 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03461. 2'-Monophosphoadenosine 5'-Diphosphoribose.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001993202 – 288Bifunctional protein MdtAAdd BLAST287

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi272630.MexAM1_META1p1728.

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi17 – 25Combined sources9
Beta strandi29 – 36Combined sources8
Turni39 – 41Combined sources3
Helixi42 – 50Combined sources9
Helixi55 – 60Combined sources6
Beta strandi61 – 66Combined sources6
Helixi70 – 83Combined sources14
Beta strandi91 – 94Combined sources4
Helixi96 – 98Combined sources3
Helixi99 – 113Combined sources15
Beta strandi122 – 126Combined sources5
Turni127 – 129Combined sources3
Helixi131 – 142Combined sources12
Beta strandi146 – 153Combined sources8
Helixi154 – 168Combined sources15
Beta strandi173 – 176Combined sources4
Helixi180 – 186Combined sources7
Turni187 – 189Combined sources3
Beta strandi191 – 195Combined sources5
Helixi206 – 209Combined sources4
Beta strandi217 – 220Combined sources4
Beta strandi224 – 226Combined sources3
Beta strandi237 – 241Combined sources5
Beta strandi244 – 247Combined sources4
Helixi249 – 267Combined sources19
Beta strandi274 – 276Combined sources3
Helixi277 – 287Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LU9X-ray1.90A/B/C2-288[»]
1LUAX-ray1.90A/B/C2-288[»]
ProteinModelPortaliP55818.
SMRiP55818.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55818.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4108N1H. Bacteria.
ENOG410XT65. LUCA.
HOGENOMiHOG000236834.
OMAiFFGPMRV.

Family and domain databases

CDDicd01078. NAD_bind_H4MPT_DH. 1 hit.
Gene3Di3.40.50.10280. 1 hit.
InterProiView protein in InterPro
IPR015259. Methyl-teptahyd_DH_N.
IPR037089. Methyl-teptahyd_DH_N_sf.
IPR036291. NAD(P)-bd_dom_sf.
IPR035015. NAD-bd_H4MPT_DH.
PfamiView protein in Pfam
PF09176. Mpt_N. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P55818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKLLFQFD TDATPSVFDV VVGYDGGADH ITGYGNVTPD NVGAYVDGTI
60 70 80 90 100
YTRGGKEKQS TAIFVGGGDM AAGERVFEAV KKRFFGPFRV SCMLDSNGSN
110 120 130 140 150
TTAAAGVALV VKAAGGSVKG KKAVVLAGTG PVGMRSAALL AGEGAEVVLC
160 170 180 190 200
GRKLDKAQAA ADSVNKRFKV NVTAAETADD ASRAEAVKGA HFVFTAGAIG
210 220 230 240 250
LELLPQAAWQ NESSIEIVAD YNAQPPLGIG GIDATDKGKE YGGKRAFGAL
260 270 280
GIGGLKLKLH RACIAKLFES SEGVFDAEEI YKLAKEMA
Length:288
Mass (Da):29,736
Last modified:January 23, 2007 - v3
Checksum:i36519D60F8F8E830
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27235 Genomic DNA. No translation available.
CP001510 Genomic DNA. Translation: ACS39572.1.
RefSeqiWP_003597637.1. NC_012808.1.

Genome annotation databases

EnsemblBacteriaiACS39572; ACS39572; MexAM1_META1p1728.
KEGGimea:Mex_1p1728.

Similar proteinsi

Entry informationi

Entry nameiMTDA_METEA
AccessioniPrimary (citable) accession number: P55818
Secondary accession number(s): C5B108
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 107 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references