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P38539

- DHM1_METME

UniProt

P38539 - DHM1_METME

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Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene
N/A
Organism
Methylophilus methylotrophus (Bacterium W3A1)
Status
Reviewed - 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 Ca(2+) 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi173 – 1731Calcium
Metal bindingi257 – 2571Calcium
Active sitei299 – 2991Proton acceptor

GO - Molecular functioni

  1. 2-chloroethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro
  3. ethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
  4. methanol ferricytochrome-c oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. methanol metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

Calcium, Metal-binding, PQQ

Enzyme and pathway databases

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

Cell inner membrane; Peripheral membrane protein; Periplasmic side
Note: Periplasmic, but associated with inner membrane.

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 573573Methanol dehydrogenase [cytochrome c] subunit 1PRO_0000205342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
573
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Turni36 – 383Combined sources
Helixi39 – 413Combined sources
Beta strandi43 – 497Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 705Combined sources
Turni73 – 753Combined sources
Beta strandi77 – 815Combined sources
Beta strandi87 – 926Combined sources
Helixi98 – 1036Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi127 – 1337Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1446Combined sources
Helixi148 – 1503Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi164 – 1685Combined sources
Helixi172 – 1743Combined sources
Beta strandi179 – 1846Combined sources
Turni185 – 1873Combined sources
Beta strandi190 – 1989Combined sources
Helixi200 – 2034Combined sources
Turni207 – 2126Combined sources
Helixi214 – 2163Combined sources
Helixi221 – 2244Combined sources
Helixi230 – 2334Combined sources
Beta strandi243 – 2453Combined sources
Turni246 – 2494Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi259 – 2613Combined sources
Helixi263 – 2653Combined sources
Turni271 – 2744Combined sources
Beta strandi275 – 2806Combined sources
Turni281 – 2833Combined sources
Beta strandi286 – 2938Combined sources
Beta strandi307 – 3137Combined sources
Beta strandi316 – 3249Combined sources
Beta strandi328 – 3347Combined sources
Turni335 – 3373Combined sources
Beta strandi340 – 3478Combined sources
Beta strandi352 – 3565Combined sources
Turni358 – 3603Combined sources
Beta strandi362 – 3654Combined sources
Helixi367 – 3693Combined sources
Beta strandi377 – 3826Combined sources
Beta strandi394 – 3963Combined sources
Turni397 – 4004Combined sources
Beta strandi401 – 4077Combined sources
Beta strandi409 – 4157Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi446 – 4516Combined sources
Turni453 – 4553Combined sources
Beta strandi458 – 4669Combined sources
Beta strandi473 – 4753Combined sources
Turni476 – 4783Combined sources
Beta strandi479 – 4835Combined sources
Beta strandi487 – 4937Combined sources
Turni494 – 4963Combined sources
Beta strandi499 – 5046Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi521 – 5288Combined sources
Turni532 – 5354Combined sources
Helixi536 – 5394Combined sources
Helixi547 – 5504Combined sources
Helixi551 – 5544Combined sources
Turni555 – 5573Combined sources
Helixi558 – 5603Combined sources
Beta strandi567 – 5726Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-573.
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. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF01011. PQQ. 5 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 .
PIRi S68591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G72 X-ray 1.90 A/C 1-573 [» ]
2AD6 X-ray 1.50 A/C 3-573 [» ]
2AD7 X-ray 1.50 A/C 3-573 [» ]
2AD8 X-ray 1.60 A/C 3-573 [» ]
4AAH X-ray 2.40 A/C 3-573 [» ]
ProteinModelPortali P38539.
SMRi P38539. Positions 3-573.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P38539.

Miscellaneous databases

EvolutionaryTracei P38539.

Family and domain databases

Gene3Di 2.140.10.10. 1 hit.
InterProi IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view ]
Pfami PF01011. PQQ. 5 hits.
[Graphical view ]
SMARTi SM00564. PQQ. 4 hits.
[Graphical view ]
SUPFAMi SSF50998. SSF50998. 1 hit.
TIGRFAMsi TIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEi PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1."
    Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.
    J. Mol. Biol. 259:480-501(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  2. "Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes."
    Anthony C.
    Antioxid. Redox Signal. 3:757-774(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "The active site structure of the calcium-containing quinoprotein methanol dehydrogenase."
    White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F., Davidson V.L.
    Biochemistry 32:12955-12958(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  4. "The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution."
    Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A., Mathews F.S.
    J. Biol. Chem. 267:22289-22297(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

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 26, 2014
This is version 104 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

External Data

Dasty 3