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Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene
N/A
Organism
Methylophilus methylotrophus (Bacterium W3A1)
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+.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.
  • pyrroloquinoline quinoneNote: Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi173Calcium1
Metal bindingi257Calcium1
Active sitei299Proton 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

BRENDAi1.1.2.7. 3319.
1.2.2.B2. 3319.
SABIO-RKP38539.

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
OrganismiMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifieri17 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002053421 – 573Methanol dehydrogenase [cytochrome c] subunit 1Add BLAST573

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi105 ↔ 106
Disulfide bondi146 ↔ 169
Disulfide bondi381 ↔ 410

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterotetramer of 2 alpha and 2 beta subunits.

Structurei

Secondary structure

1573
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Turni36 – 38Combined sources3
Helixi39 – 41Combined sources3
Beta strandi43 – 49Combined sources7
Beta strandi61 – 63Combined sources3
Beta strandi66 – 70Combined sources5
Turni73 – 75Combined sources3
Beta strandi77 – 81Combined sources5
Beta strandi87 – 92Combined sources6
Helixi98 – 103Combined sources6
Beta strandi114 – 116Combined sources3
Beta strandi119 – 123Combined sources5
Beta strandi127 – 133Combined sources7
Turni134 – 136Combined sources3
Beta strandi139 – 144Combined sources6
Helixi148 – 150Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi164 – 168Combined sources5
Helixi172 – 174Combined sources3
Beta strandi179 – 184Combined sources6
Turni185 – 187Combined sources3
Beta strandi190 – 198Combined sources9
Helixi200 – 203Combined sources4
Turni207 – 212Combined sources6
Helixi214 – 216Combined sources3
Helixi221 – 224Combined sources4
Helixi230 – 233Combined sources4
Beta strandi243 – 245Combined sources3
Turni246 – 249Combined sources4
Beta strandi250 – 254Combined sources5
Beta strandi259 – 261Combined sources3
Helixi263 – 265Combined sources3
Turni271 – 274Combined sources4
Beta strandi275 – 280Combined sources6
Turni281 – 283Combined sources3
Beta strandi286 – 293Combined sources8
Beta strandi307 – 313Combined sources7
Beta strandi316 – 324Combined sources9
Beta strandi328 – 334Combined sources7
Turni335 – 337Combined sources3
Beta strandi340 – 347Combined sources8
Beta strandi352 – 356Combined sources5
Turni358 – 360Combined sources3
Beta strandi362 – 365Combined sources4
Helixi367 – 369Combined sources3
Beta strandi377 – 382Combined sources6
Beta strandi394 – 396Combined sources3
Turni397 – 400Combined sources4
Beta strandi401 – 407Combined sources7
Beta strandi409 – 415Combined sources7
Beta strandi429 – 435Combined sources7
Beta strandi446 – 451Combined sources6
Turni453 – 455Combined sources3
Beta strandi458 – 466Combined sources9
Beta strandi473 – 475Combined sources3
Turni476 – 478Combined sources3
Beta strandi479 – 483Combined sources5
Beta strandi487 – 493Combined sources7
Turni494 – 496Combined sources3
Beta strandi499 – 504Combined sources6
Beta strandi514 – 518Combined sources5
Beta strandi521 – 528Combined sources8
Turni532 – 535Combined sources4
Helixi536 – 539Combined sources4
Helixi547 – 550Combined sources4
Helixi551 – 554Combined sources4
Turni555 – 557Combined sources3
Helixi558 – 560Combined sources3
Beta strandi567 – 572Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90A/C1-573[»]
2AD6X-ray1.50A/C3-573[»]
2AD7X-ray1.50A/C3-573[»]
2AD8X-ray1.60A/C3-573[»]
4AAHX-ray2.40A/C3-573[»]
ProteinModelPortaliP38539.
SMRiP38539.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38539.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

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]
PfamiPF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 4 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38539-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADADLDKQV NTAGAWPIAT GGYYSQHNSP LAQINKSNVK NVKAAWSFST
60 70 80 90 100
GVLNGHEGAP LVIGDMMYVH SAFPNNTYAL NLNDPGKIVW QHKPKQDAST
110 120 130 140 150
KAVMCCDVVD RGLAYGAGQI VKKQANGHLL ALDAKTGKIN WEVEVCDPKV
160 170 180 190 200
GSTLTQAPFV AKDTVLMGCS GAELGVRGAV NAFDLKTGEL KWRAFATGSD
210 220 230 240 250
DSVRLAKDFN SANPHYGQFG LGTKTWEGDA WKIGGGTNWG WYAYDPKLNL
260 270 280 290 300
FYYGSGNPAP WNETMRPGDN KWTMTIWGRD LDTGMAKWGY QKTPHDEWDF
310 320 330 340 350
AGVNQMVLTD QPVNGKMTPL LSHIDRNGIL YTLNRENGNL IVAEKVDPAV
360 370 380 390 400
NVFKKVDLKT GTPVRDPEFA TRMDHKGTNI CPSAMGFHNQ GVDSYDPESR
410 420 430 440 450
TLYAGLNHIC MDWEPFMLPY RAGQFFVGAT LAMYPGPNGP TKKEMGQIRA
460 470 480 490 500
FDLTTGKAKW TKWEKFAAWG GTLYTKGGLV WYATLDGYLK ALDNKDGKEL
510 520 530 540 550
WNFKMPSGGI GSPMTYSFKG KQYIGSMYGV GGWPGVGLVF DLTDPSAGLG
560 570
AVGAFRELQN HTQMGGGLMV FSL
Length:573
Mass (Da):62,635
Last modified:November 8, 2002 - v2
Checksum:iA06C9B3091BB8F0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41040 Genomic DNA. Translation: AAA83765.1.
PIRiS68591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41040 Genomic DNA. Translation: AAA83765.1.
PIRiS68591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90A/C1-573[»]
2AD6X-ray1.50A/C3-573[»]
2AD7X-ray1.50A/C3-573[»]
2AD8X-ray1.60A/C3-573[»]
4AAHX-ray2.40A/C3-573[»]
ProteinModelPortaliP38539.
SMRiP38539.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.2.7. 3319.
1.2.2.B2. 3319.
SABIO-RKP38539.

Miscellaneous databases

EvolutionaryTraceiP38539.

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]
PfamiPF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 4 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHM1_METME
AccessioniPrimary (citable) accession number: P38539
Secondary accession number(s): Q59540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 8, 2002
Last modified: November 2, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.