Reviewed, UniProtKB/Swiss-Prot P16027 (DHM1_METEA)

Names and origin

Protein names

Recommended name:
    Methanol dehydrogenase subunit 1
    EC=1.1.99.8
Alternative name(s):
    MDH large subunit alpha
    MEDH

Gene names

Name:	moxF
Synonyms:	mxaF
Ordered Locus Names:	MexAM1_META1p4538

Organism

Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]

Taxonomic identifier

272630 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	A primary alcohol + acceptor = an aldehyde + reduced acceptor.
Cofactor	Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270. Binds 1 calcium ion per subunit.
Subunit structure	Heterotetramer composed of 2 alpha and 2 beta subunits.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note: Periplasmic, but associated with inner membrane.
Sequence similarities	Belongs to the bacterial PQQ dehydrogenase family.

Ontologies

Keywords
Biological process	Methanol utilization
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond PQQ
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methanol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Ref.3

Chain

28 – 626

599

Methanol dehydrogenase subunit 1

PRO_0000025566

Sites

Active site

330

1

Proton acceptor By similarity

Metal binding

204

1

Calcium

Metal binding

288

1

Calcium

Amino acid modifications

Disulfide bond

130 ↔ 131

Ref.5

Disulfide bond

413 ↔ 442

Ref.5

Experimental info

Mutagenesis

130

1

C → S: Inactive. Ref.7

Mutagenesis

131

1

C → S: Inactive. Ref.7

Mutagenesis

330

1

D → E: Lower affinity for methanol. Ref.7

Secondary structure

1

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626

Helix Strand Turn

Details...

Helix

29 – 35

7

Turn

61 – 63

3

Helix

64 – 66

3

Beta strand

67 – 74

8

Beta strand

86 – 88

3

Beta strand

91 – 95

5

Turn

98 – 100

3

Beta strand

102 – 106

5

Beta strand

112 – 117

6

Helix

123 – 128

6

Beta strand

139 – 141

3

Beta strand

145 – 147

3

Beta strand

150 – 154

5

Beta strand

158 – 164

7

Turn

165 – 167

3

Beta strand

170 – 175

6

Helix

179 – 181

3

Beta strand

190 – 192

3

Beta strand

195 – 198

4

Helix

203 – 205

3

Beta strand

210 – 215

6

Turn

216 – 218

3

Beta strand

221 – 229

9

Helix

231 – 234

4

Turn

238 – 243

6

Helix

245 – 247

3

Helix

252 – 255

4

Helix

261 – 264

4

Turn

277 – 279

3

Beta strand

281 – 285

5

Helix

294 – 296

3

Beta strand

304 – 311

8

Turn

312 – 314

3

Beta strand

317 – 324

8

Beta strand

338 – 343

6

Beta strand

349 – 356

8

Beta strand

360 – 366

7

Turn

367 – 369

3

Beta strand

372 – 379

8

Beta strand

384 – 388

5

Turn

390 – 392

3

Beta strand

395 – 397

3

Helix

399 – 401

3

Beta strand

409 – 414

6

Beta strand

426 – 428

3

Turn

429 – 432

4

Beta strand

433 – 439

7

Beta strand

441 – 447

7

Beta strand

461 – 467

7

Turn

473 – 476

4

Beta strand

480 – 485

6

Turn

487 – 489

3

Beta strand

492 – 500

9

Beta strand

507 – 509

3

Turn

510 – 512

3

Beta strand

513 – 517

5

Beta strand

521 – 527

7

Turn

528 – 530

3

Beta strand

533 – 538

6

Beta strand

548 – 552

5

Beta strand

555 – 562

8

Turn

566 – 569

4

Helix

570 – 574

5

Helix

582 – 584

3

Helix

585 – 588

4

Turn

589 – 591

3

Helix

592 – 594

3

Beta strand

601 – 607

7

Turn

616 – 619

4

Sequences

	Sequence		Length	Mass (Da)
	P16027-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 64988D0AFD2AD34C	FASTA	626	68,434
	10 20 30 40 50 60 MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN 70 80 90 100 110 120 KGNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYIHTSFPN NTFALGLDDP GTILWQDKPK 130 140 150 160 170 180 QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDGNV AALNAETGET VWKVENSDIK 190 200 210 220 230 240 VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGE QVWRAYATGP DKDLLLASDF 250 260 270 280 290 300 NIKNPHYGQK GLGTGTWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD 310 320 330 340 350 360 NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMLS EQKDKDGKAR KLLTHPDRNG 370 380 390 400 410 420 IVYTLDRTDG ALVSANKLDD TVNVFKSVDL KTGQPVRDPE YGTRMDHLAK DICPSAMGYH 430 440 450 460 470 480 NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG 490 500 510 520 530 540 QIKAYNAITG DYKWEKMERF AVWGGTMATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP 550 560 570 580 590 600 SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQMGG 610 620 GVVVFSLDGK GPYDDPNVGE WKSAAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ genes involved in methanol oxidation." Anderson D.J., Morris C.J., Nunn D.N., Anthony C., Lidstrom M.E. Gene 90:173-176(1990) [PubMed: 2116368] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources." Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E. PLoS ONE 4:E5584-E5584(2009) [PubMed: 19440302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1." Nunn D.N., Day D., Anthony C. Biochem. J. 260:857-862(1989) [PubMed: 2504152] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-53.
[4]	"Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes." Anthony C. Antioxid. Redox Signal. 3:757-774(2001) [PubMed: 11761326] [Abstract] Cited for: REVIEW.
[5]	"The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues." Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C. Nat. Struct. Biol. 1:102-105(1994) [PubMed: 7656012] [Abstract] Cited for: DISULFIDE BONDS.
[6]	"The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A." Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C. Structure 3:177-187(1995) [PubMed: 7735834] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
[7]	"Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)." Afolabi P.R., Mohammed F., Amaratunga K., Majekodunmi O., Dales S.L., Gill R., Thompson D., Cooper J.B., Wood S.P., Goodwin P.M., Anthony C. Biochemistry 40:9799-9809(2001) [PubMed: 11502173] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT GLU-330, MUTAGENESIS OF CYS-130; CYS-131 AND ASP-330.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M31108 Genomic DNA. Translation: AAA25380.1.
CP001510 Genomic DNA. Translation: ACS42169.1. Different initiation.

PIR

JQ0706.

RefSeq

YP_002965446.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H4I	X-ray	1.94	A/C	28-626	[»]
1H4J	X-ray	3.00	A/C/E/G	28-626	[»]
1W6S	X-ray	1.20	A/C	28-626	[»]

ModBase

Search...

Genome annotation databases

GeneID

7994324.

Organism-specific databases

CMR

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3921.

BRENDA

1.1.99.8. 20440.

Family and domain databases

InterPro

IPR019556. PQQ-dependent_C.
IPR019551. PQQ-dependent_N.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR011047. Quino_AlcDH-like.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]

Gene3D

G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.

Pfam

PF01011. PQQ. 5 hits.
PF10535. PQQ_C. 1 hit.
PF10527. PQQ_N. 1 hit.
[Graphical view]

SMART

SM00564. PQQ. 3 hits.
[Graphical view]

TIGRFAMs

TIGR03075. PQQ_enz_alc_DH. 1 hit.

PROSITE

PS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHM1_METEA

Accession

Primary (citable) accession number: P16027
Secondary accession number(s): C5AQA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 24, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)