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Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene

moxF

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of primary alcohols including methanol.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Calcium
Metal bindingi293 – 2931Calcium
Active sitei335 – 3351Proton acceptor

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-3923.
BRENDAi1.1.2.B2. 3341.

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
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 631599Methanol dehydrogenase [cytochrome c] subunit 1PRO_0000025568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 1361 Publication
Disulfide bondi418 ↔ 4471 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi318586.Pden_2993.

Structurei

Secondary structure

1
631
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 407Combined sources
Turni66 – 683Combined sources
Helixi69 – 713Combined sources
Beta strandi72 – 798Combined sources
Beta strandi91 – 933Combined sources
Beta strandi96 – 994Combined sources
Turni103 – 1053Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi117 – 1226Combined sources
Helixi128 – 1336Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi163 – 1697Combined sources
Turni170 – 1723Combined sources
Beta strandi175 – 1806Combined sources
Helixi184 – 1863Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi200 – 2034Combined sources
Helixi208 – 2103Combined sources
Beta strandi215 – 2206Combined sources
Turni221 – 2233Combined sources
Beta strandi226 – 2349Combined sources
Helixi236 – 2394Combined sources
Turni243 – 2464Combined sources
Helixi250 – 2523Combined sources
Helixi257 – 2604Combined sources
Helixi266 – 2694Combined sources
Beta strandi279 – 2813Combined sources
Turni282 – 2854Combined sources
Beta strandi286 – 2905Combined sources
Helixi299 – 3013Combined sources
Turni307 – 3104Combined sources
Beta strandi311 – 3166Combined sources
Turni317 – 3193Combined sources
Beta strandi322 – 3298Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi354 – 3618Combined sources
Beta strandi365 – 3717Combined sources
Turni372 – 3743Combined sources
Beta strandi377 – 3848Combined sources
Beta strandi389 – 3935Combined sources
Turni395 – 3973Combined sources
Beta strandi400 – 4023Combined sources
Helixi404 – 4063Combined sources
Beta strandi414 – 4196Combined sources
Beta strandi431 – 4333Combined sources
Turni434 – 4374Combined sources
Beta strandi438 – 4447Combined sources
Beta strandi446 – 4527Combined sources
Beta strandi466 – 4727Combined sources
Turni477 – 4804Combined sources
Beta strandi484 – 4907Combined sources
Turni491 – 4944Combined sources
Beta strandi495 – 50410Combined sources
Beta strandi508 – 5136Combined sources
Turni514 – 5163Combined sources
Beta strandi517 – 5215Combined sources
Beta strandi525 – 5317Combined sources
Turni532 – 5343Combined sources
Beta strandi537 – 5426Combined sources
Beta strandi552 – 5565Combined sources
Beta strandi559 – 5668Combined sources
Helixi570 – 5778Combined sources
Helixi585 – 5928Combined sources
Turni593 – 5953Combined sources
Helixi596 – 5983Combined sources
Beta strandi605 – 6117Combined sources
Turni620 – 6234Combined sources
Beta strandi627 – 6293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRWX-ray2.50A/C33-631[»]
ProteinModelPortaliP12293.
SMRiP12293. Positions 33-631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12293.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41089S2. Bacteria.
COG4993. LUCA.

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. 4 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.

P12293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRNTPKARG ASSLAMAVAM GLAVLTTAPA TANDQLVELA KDPANWVMTG
60 70 80 90 100
RDYNAQNYSE MTDINKENVK QLRPAWSFST GVLHGHEGTP LVVGDRMFIH
110 120 130 140 150
TPFPNTTFAL DLNEPGKILW QNKPKQNPTA RTVACCDVVN RGLAYWPGDD
160 170 180 190 200
QVKPLIFRTQ LDGHIVAMDA ETGETRWIME NSDIKVGSTL TIAPYVIKDL
210 220 230 240 250
VLVGSSGAEL GVRGYVTAYD VKSGEMRWRA FATGPDEELL LAEDFNAPNP
260 270 280 290 300
HYGQKNLGLE TWEGDAWKIG GGTNWGWYAY DPEVDLFYYG SGNPAPWNET
310 320 330 340 350
MRPGDNKWTM AIWGREATTG EAKFAYQKTP HDEWDYAGVN VMMLSEQEDK
360 370 380 390 400
QGQMRKLLTH PDRNGIVYTL DRTNGDLISA DKMDDTVNWV KEVQLDTGLP
410 420 430 440 450
VRDPEFGTRM DHKARDICPS AMGYHNQGHD SYDPERKVFM LGINHICMDW
460 470 480 490 500
EPFMLPYRAG QFFVGATLTM YPGPKATAER AGAGQIKAYD AISGEMKWEK
510 520 530 540 550
MERFSVWGGT MATAGGLTFY VTLDGFIKAR DSDTGDLLWK FKLPSGVIGH
560 570 580 590 600
PMTYKHDGRQ YVAIMYGVGG WPGVGLVFDL ADPTAGLGSV GAFKRLQEFT
610 620 630
QMGGGVMVFS LDGESPYSDP NVGEYAPGEP T
Length:631
Mass (Da):69,799
Last modified:October 1, 1989 - v1
Checksum:i0934DC93FFC5730B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17339 Genomic DNA. Translation: AAA88366.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17339 Genomic DNA. Translation: AAA88366.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRWX-ray2.50A/C33-631[»]
ProteinModelPortaliP12293.
SMRiP12293. Positions 33-631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318586.Pden_2993.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG41089S2. Bacteria.
COG4993. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3923.
BRENDAi1.1.2.B2. 3341.

Miscellaneous databases

EvolutionaryTraceiP12293.

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. 4 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_PARDE
AccessioniPrimary (citable) accession number: P12293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 9, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

MDH is the major protein in the cell during growth on methanol (in P.denitrificans MDH constitutes up to 15% of the total cell protein).

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.