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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)DescriptionActionsGraphical viewLength
Metal bindingi209Calcium1
Metal bindingi293Calcium1
Active sitei335Proton acceptor1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 321 PublicationAdd BLAST32
ChainiPRO_000002556833 – 631Methanol dehydrogenase [cytochrome c] subunit 1Add BLAST599

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1631
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 40Combined sources7
Turni66 – 68Combined sources3
Helixi69 – 71Combined sources3
Beta strandi72 – 79Combined sources8
Beta strandi91 – 93Combined sources3
Beta strandi96 – 99Combined sources4
Turni103 – 105Combined sources3
Beta strandi107 – 111Combined sources5
Beta strandi117 – 122Combined sources6
Helixi128 – 133Combined sources6
Beta strandi144 – 146Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi155 – 159Combined sources5
Beta strandi163 – 169Combined sources7
Turni170 – 172Combined sources3
Beta strandi175 – 180Combined sources6
Helixi184 – 186Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi200 – 203Combined sources4
Helixi208 – 210Combined sources3
Beta strandi215 – 220Combined sources6
Turni221 – 223Combined sources3
Beta strandi226 – 234Combined sources9
Helixi236 – 239Combined sources4
Turni243 – 246Combined sources4
Helixi250 – 252Combined sources3
Helixi257 – 260Combined sources4
Helixi266 – 269Combined sources4
Beta strandi279 – 281Combined sources3
Turni282 – 285Combined sources4
Beta strandi286 – 290Combined sources5
Helixi299 – 301Combined sources3
Turni307 – 310Combined sources4
Beta strandi311 – 316Combined sources6
Turni317 – 319Combined sources3
Beta strandi322 – 329Combined sources8
Beta strandi343 – 348Combined sources6
Beta strandi354 – 361Combined sources8
Beta strandi365 – 371Combined sources7
Turni372 – 374Combined sources3
Beta strandi377 – 384Combined sources8
Beta strandi389 – 393Combined sources5
Turni395 – 397Combined sources3
Beta strandi400 – 402Combined sources3
Helixi404 – 406Combined sources3
Beta strandi414 – 419Combined sources6
Beta strandi431 – 433Combined sources3
Turni434 – 437Combined sources4
Beta strandi438 – 444Combined sources7
Beta strandi446 – 452Combined sources7
Beta strandi466 – 472Combined sources7
Turni477 – 480Combined sources4
Beta strandi484 – 490Combined sources7
Turni491 – 494Combined sources4
Beta strandi495 – 504Combined sources10
Beta strandi508 – 513Combined sources6
Turni514 – 516Combined sources3
Beta strandi517 – 521Combined sources5
Beta strandi525 – 531Combined sources7
Turni532 – 534Combined sources3
Beta strandi537 – 542Combined sources6
Beta strandi552 – 556Combined sources5
Beta strandi559 – 566Combined sources8
Helixi570 – 577Combined sources8
Helixi585 – 592Combined sources8
Turni593 – 595Combined sources3
Helixi596 – 598Combined sources3
Beta strandi605 – 611Combined sources7
Turni620 – 623Combined sources4
Beta strandi627 – 629Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRWX-ray2.50A/C33-631[»]
ProteinModelPortaliP12293.
SMRiP12293.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRWX-ray2.50A/C33-631[»]
ProteinModelPortaliP12293.
SMRiP12293.
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: November 2, 2016
This is version 109 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.