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Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene

moxF

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 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)DescriptionActionsGraphical viewLength
Metal bindingi204Calcium1
Metal bindingi288Calcium1
Active sitei330Proton acceptorBy similarity1

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.
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 / JCM 2805 / NCIMB 9133 / 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)DescriptionActionsGraphical viewLength
Mutagenesisi130C → S: Inactive. 1 Publication1
Mutagenesisi131C → S: Inactive. 1 Publication1
Mutagenesisi330D → E: Lower affinity for methanol. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000002556628 – 626Methanol dehydrogenase [cytochrome c] subunit 1Add BLAST599

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 35Combined sources7
Turni61 – 63Combined sources3
Helixi64 – 66Combined sources3
Beta strandi67 – 74Combined sources8
Beta strandi86 – 88Combined sources3
Beta strandi91 – 95Combined sources5
Turni98 – 100Combined sources3
Beta strandi102 – 106Combined sources5
Beta strandi112 – 117Combined sources6
Helixi123 – 128Combined sources6
Beta strandi139 – 141Combined sources3
Beta strandi145 – 147Combined sources3
Beta strandi150 – 154Combined sources5
Beta strandi158 – 164Combined sources7
Turni165 – 167Combined sources3
Beta strandi170 – 175Combined sources6
Helixi179 – 181Combined sources3
Beta strandi190 – 192Combined sources3
Beta strandi195 – 198Combined sources4
Helixi203 – 205Combined sources3
Beta strandi210 – 215Combined sources6
Turni216 – 218Combined sources3
Beta strandi221 – 229Combined sources9
Helixi231 – 234Combined sources4
Turni238 – 243Combined sources6
Helixi245 – 247Combined sources3
Helixi252 – 255Combined sources4
Helixi261 – 264Combined sources4
Beta strandi274 – 276Combined sources3
Turni277 – 279Combined sources3
Beta strandi281 – 285Combined sources5
Helixi294 – 296Combined sources3
Beta strandi304 – 311Combined sources8
Turni312 – 314Combined sources3
Beta strandi317 – 324Combined sources8
Beta strandi338 – 343Combined sources6
Beta strandi349 – 356Combined sources8
Beta strandi360 – 366Combined sources7
Turni367 – 369Combined sources3
Beta strandi372 – 379Combined sources8
Beta strandi384 – 388Combined sources5
Turni390 – 392Combined sources3
Beta strandi395 – 397Combined sources3
Helixi399 – 401Combined sources3
Beta strandi409 – 414Combined sources6
Beta strandi426 – 428Combined sources3
Turni429 – 432Combined sources4
Beta strandi433 – 439Combined sources7
Beta strandi441 – 447Combined sources7
Beta strandi461 – 467Combined sources7
Turni473 – 476Combined sources4
Beta strandi480 – 485Combined sources6
Turni487 – 489Combined sources3
Beta strandi492 – 500Combined sources9
Beta strandi507 – 509Combined sources3
Turni510 – 512Combined sources3
Beta strandi513 – 517Combined sources5
Beta strandi521 – 527Combined sources7
Turni528 – 530Combined sources3
Beta strandi533 – 538Combined sources6
Beta strandi548 – 552Combined sources5
Beta strandi555 – 562Combined sources8
Turni566 – 569Combined sources4
Helixi570 – 574Combined sources5
Turni579 – 581Combined sources3
Helixi582 – 584Combined sources3
Helixi585 – 588Combined sources4
Turni589 – 591Combined sources3
Helixi592 – 594Combined sources3
Beta strandi601 – 607Combined sources7
Helixi612 – 614Combined sources3
Turni616 – 619Combined sources4

3D structure databases

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

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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94A/C28-626[»]
1H4JX-ray3.00A/C/E/G28-626[»]
1W6SX-ray1.20A/C28-626[»]
ProteinModelPortaliP16027.
SMRiP16027.
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.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3921.
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...

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: November 2, 2016
This is version 130 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.