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Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene

moxF

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

Functioni

Catalyzes the oxidation of primary alcohols including methanol.

Catalytic activityi

A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinoneNote: Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270.
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041Calcium
Metal bindingi288 – 2881Calcium
Active sitei330 – 3301Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

Calcium, Metal-binding, PQQ

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3921.
MEXT272630:GBY6-4283-MONOMER.
BRENDAi1.1.2.7. 3296.

Names & Taxonomyi

Protein namesi
Recommended name:
Methanol dehydrogenase [cytochrome c] subunit 1 (EC:1.1.2.7)
Alternative name(s):
MDH large subunit alpha
MEDH
Gene namesi
Name:moxF
Synonyms:mxaF
Ordered Locus Names:MexAM1_META1p4538
OrganismiMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
Taxonomic identifieri272630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
Proteomesi
  • UP000009081 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301C → S: Inactive. 1 Publication
Mutagenesisi131 – 1311C → S: Inactive. 1 Publication
Mutagenesisi330 – 3301D → E: Lower affinity for methanol. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 626599Methanol dehydrogenase [cytochrome c] subunit 1PRO_0000025566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi130 ↔ 1311 Publication
Disulfide bondi413 ↔ 4421 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterotetramer composed of 2 alpha and 2 beta subunits.1 Publication

Protein-protein interaction databases

STRINGi272630.MexAM1_META1p4538.

Structurei

Secondary structure

1
626
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357Combined sources
Turni61 – 633Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 748Combined sources
Beta strandi86 – 883Combined sources
Beta strandi91 – 955Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi112 – 1176Combined sources
Helixi123 – 1286Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi158 – 1647Combined sources
Turni165 – 1673Combined sources
Beta strandi170 – 1756Combined sources
Helixi179 – 1813Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi195 – 1984Combined sources
Helixi203 – 2053Combined sources
Beta strandi210 – 2156Combined sources
Turni216 – 2183Combined sources
Beta strandi221 – 2299Combined sources
Helixi231 – 2344Combined sources
Turni238 – 2436Combined sources
Helixi245 – 2473Combined sources
Helixi252 – 2554Combined sources
Helixi261 – 2644Combined sources
Beta strandi274 – 2763Combined sources
Turni277 – 2793Combined sources
Beta strandi281 – 2855Combined sources
Helixi294 – 2963Combined sources
Beta strandi304 – 3118Combined sources
Turni312 – 3143Combined sources
Beta strandi317 – 3248Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi349 – 3568Combined sources
Beta strandi360 – 3667Combined sources
Turni367 – 3693Combined sources
Beta strandi372 – 3798Combined sources
Beta strandi384 – 3885Combined sources
Turni390 – 3923Combined sources
Beta strandi395 – 3973Combined sources
Helixi399 – 4013Combined sources
Beta strandi409 – 4146Combined sources
Beta strandi426 – 4283Combined sources
Turni429 – 4324Combined sources
Beta strandi433 – 4397Combined sources
Beta strandi441 – 4477Combined sources
Beta strandi461 – 4677Combined sources
Turni473 – 4764Combined sources
Beta strandi480 – 4856Combined sources
Turni487 – 4893Combined sources
Beta strandi492 – 5009Combined sources
Beta strandi507 – 5093Combined sources
Turni510 – 5123Combined sources
Beta strandi513 – 5175Combined sources
Beta strandi521 – 5277Combined sources
Turni528 – 5303Combined sources
Beta strandi533 – 5386Combined sources
Beta strandi548 – 5525Combined sources
Beta strandi555 – 5628Combined sources
Turni566 – 5694Combined sources
Helixi570 – 5745Combined sources
Turni579 – 5813Combined sources
Helixi582 – 5843Combined sources
Helixi585 – 5884Combined sources
Turni589 – 5913Combined sources
Helixi592 – 5943Combined sources
Beta strandi601 – 6077Combined sources
Helixi612 – 6143Combined sources
Turni616 – 6194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94A/C28-626[»]
1H4JX-ray3.00A/C/E/G28-626[»]
1W6SX-ray1.20A/C28-626[»]
ProteinModelPortaliP16027.
SMRiP16027. Positions 28-622.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16027.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41089S2. Bacteria.
COG4993. LUCA.
HOGENOMiHOG000217982.
KOiK14028.
OrthoDBiEOG6FNHJ2.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF01011. PQQ. 1 hit.
PF13360. PQQ_2. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 3 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS
60 70 80 90 100
NNFSDLKQIN KGNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYIHTSFPN
110 120 130 140 150
NTFALGLDDP GTILWQDKPK QNPAARAVAC CDLVNRGLAY WPGDGKTPAL
160 170 180 190 200
ILKTQLDGNV AALNAETGET VWKVENSDIK VGSTLTIAPY VVKDKVIIGS
210 220 230 240 250
SGAELGVRGY LTAYDVKTGE QVWRAYATGP DKDLLLASDF NIKNPHYGQK
260 270 280 290 300
GLGTGTWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD
310 320 330 340 350
NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMLS EQKDKDGKAR
360 370 380 390 400
KLLTHPDRNG IVYTLDRTDG ALVSANKLDD TVNVFKSVDL KTGQPVRDPE
410 420 430 440 450
YGTRMDHLAK DICPSAMGYH NQGHDSYDPK RELFFMGINH ICMDWEPFML
460 470 480 490 500
PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG QIKAYNAITG DYKWEKMERF
510 520 530 540 550
AVWGGTMATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP SGAIGYPMTY
560 570 580 590 600
THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQMGG
610 620
GVVVFSLDGK GPYDDPNVGE WKSAAK
Length:626
Mass (Da):68,434
Last modified:April 1, 1990 - v1
Checksum:i64988D0AFD2AD34C
GO

Sequence cautioni

The sequence ACS42169.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31108 Genomic DNA. Translation: AAA25380.1.
CP001510 Genomic DNA. Translation: ACS42169.1. Different initiation.
PIRiJQ0706.
RefSeqiWP_003599114.1. NC_012808.1.

Genome annotation databases

EnsemblBacteriaiACS42169; ACS42169; MexAM1_META1p4538.
KEGGimea:Mex_1p4538.
PATRICi22514719. VBIMetExt101010_4414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31108 Genomic DNA. Translation: AAA25380.1.
CP001510 Genomic DNA. Translation: ACS42169.1. Different initiation.
PIRiJQ0706.
RefSeqiWP_003599114.1. NC_012808.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94A/C28-626[»]
1H4JX-ray3.00A/C/E/G28-626[»]
1W6SX-ray1.20A/C28-626[»]
ProteinModelPortaliP16027.
SMRiP16027. Positions 28-622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272630.MexAM1_META1p4538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS42169; ACS42169; MexAM1_META1p4538.
KEGGimea:Mex_1p4538.
PATRICi22514719. VBIMetExt101010_4414.

Phylogenomic databases

eggNOGiENOG41089S2. Bacteria.
COG4993. LUCA.
HOGENOMiHOG000217982.
KOiK14028.
OrthoDBiEOG6FNHJ2.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3921.
MEXT272630:GBY6-4283-MONOMER.
BRENDAi1.1.2.7. 3296.

Miscellaneous databases

EvolutionaryTraceiP16027.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF01011. PQQ. 1 hit.
PF13360. PQQ_2. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 3 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ genes involved in methanol oxidation."
    Anderson D.J., Morris C.J., Nunn D.N., Anthony C., Lidstrom M.E.
    Gene 90:173-176(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14718 / DSM 1338 / AM1.
  3. "The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1."
    Nunn D.N., Day D., Anthony C.
    Biochem. J. 260:857-862(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-53, SUBUNIT.
  4. "Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes."
    Anthony C.
    Antioxid. Redox Signal. 3:757-774(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues."
    Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C.
    Nat. Struct. Biol. 1:102-105(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  6. "The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A."
    Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.
    Structure 3:177-187(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
  7. "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)."
    Afolabi P.R., Mohammed F., Amaratunga K., Majekodunmi O., Dales S.L., Gill R., Thompson D., Cooper J.B., Wood S.P., Goodwin P.M., Anthony C.
    Biochemistry 40:9799-9809(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT GLU-330, MUTAGENESIS OF CYS-130; CYS-131 AND ASP-330, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiDHM1_METEA
AccessioniPrimary (citable) accession number: P16027
Secondary accession number(s): C5AQA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 9, 2015
This is version 127 of the entry and version 1 of the sequence. [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. 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.