Reviewed, UniProtKB/Swiss-Prot Q46509 (MOP_DESGI)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidoreductase
    EC=1.2.99.7
Alternative name(s):
    Molybdenum iron sulfur protein

Gene names

Name:

mop

Organism

Desulfovibrio gigas

Taxonomic identifier

879 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	907 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.
Cofactor	Binds 1 Mo6+ ion per subunit. Binds 1 molybdopterin cytosine dinucleotide (MCD) subunit. Binds 2 2Fe-2S clusters per subunit.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aldehyde dehydrogenase (FAD-independent) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum 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

Chain

1 – 907

907

Aldehyde oxidoreductase

PRO_0000166102

Regions

Domain

2 – 79

78

2Fe-2S ferredoxin-type

Sites

Metal binding

40

1

Iron-sulfur 1 (2Fe-2S) Ref.2

Metal binding

45

1

Iron-sulfur 1 (2Fe-2S) Ref.2

Metal binding

48

1

Iron-sulfur 1 (2Fe-2S) Ref.2

Metal binding

60

1

Iron-sulfur 1 (2Fe-2S) Ref.2

Metal binding

100

1

Iron-sulfur 2 (2Fe-2S) Ref.2

Metal binding

103

1

Iron-sulfur 2 (2Fe-2S) Ref.2

Metal binding

137

1

Iron-sulfur 2 (2Fe-2S) Ref.2

Metal binding

139

1

Iron-sulfur 2 (2Fe-2S) Ref.2

Metal binding

653

1

Molybdenum

Metal binding

869

1

Molybdenum

Secondary structure

1

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907

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

11 – 17

7

Helix

23 – 29

7

Beta strand

39 – 45

7

Beta strand

49 – 52

4

Beta strand

55 – 58

4

Helix

59 – 61

3

Helix

64 – 66

3

Beta strand

72 – 74

3

Helix

76 – 79

4

Helix

87 – 95

9

Helix

104 – 115

12

Helix

123 – 132

10

Beta strand

138 – 140

3

Helix

143 – 156

14

Helix

162 – 165

4

Helix

185 – 189

5

Helix

196 – 201

6

Beta strand

208 – 214

7

Beta strand

216 – 226

11

Helix

228 – 231

4

Beta strand

236 – 240

5

Helix

242 – 244

3

Beta strand

249 – 251

3

Beta strand

267 – 270

4

Beta strand

272 – 275

4

Beta strand

281 – 289

9

Helix

290 – 297

8

Beta strand

301 – 306

6

Helix

313 – 317

5

Beta strand

330 – 341

12

Helix

343 – 349

7

Beta strand

351 – 360

10

Beta strand

372 – 377

6

Beta strand

383 – 388

6

Helix

392 – 403

12

Helix

407 – 409

3

Beta strand

410 – 414

5

Helix

423 – 425

3

Helix

430 – 440

11

Beta strand

444 – 447

4

Helix

450 – 455

6

Beta strand

463 – 471

9

Beta strand

477 – 487

11

Helix

495 – 505

11

Turn

506 – 509

4

Beta strand

514 – 522

9

Turn

533 – 536

4

Helix

537 – 555

19

Helix

559 – 566

8

Helix

585 – 606

22

Beta strand

609 – 626

18

Turn

627 – 629

3

Beta strand

631 – 638

8

Beta strand

644 – 647

4

Beta strand

653 – 655

3

Helix

657 – 669

13

Helix

670 – 672

3

Helix

676 – 678

3

Beta strand

679 – 681

3

Turn

686 – 688

3

Helix

700 – 719

20

Beta strand

724 – 726

3

Helix

729 – 734

6

Beta strand

740 – 746

7

Turn

755 – 757

3

Beta strand

766 – 778

13

Turn

779 – 781

3

Beta strand

784 – 794

11

Helix

801 – 820

20

Turn

827 – 829

3

Beta strand

830 – 832

3

Turn

833 – 837

5

Helix

841 – 843

3

Beta strand

848 – 852

5

Helix

861 – 863

3

Helix

870 – 872

3

Helix

875 – 887

13

Helix

898 – 906

9

Sequences

	Sequence		Length	Mass (Da)
	Q46509-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 898E7EEF708A64DF	FASTA	907	97,035
	10 20 30 40 50 60 MIQKVITVNG IEQNLFVDAE ALLSDVLRQQ LGLTGVKVGC EQGQCGACSV ILDGKVVRAC 70 80 90 100 110 120 VTKMKRVADG AQITTIEGVG QPENLHPLQK AWVLHGGAQC GFCSPGFIVS AKGLLDTNAD 130 140 150 160 170 180 PSREDVRDWF QKHRNACRCT GYKPLVDAVM DAAAVINGKK PETDLEFKMP ADGRIWGSKY 190 200 210 220 230 240 PRPTAVAKVT GTLDYGADLG LKMPAGTLHL AMVQAKVSHA NIKGIDTSEA LTMPGVHSVI 250 260 270 280 290 300 THKDVKGKNR ITGLITFPTN KGDGWDRPIL CDEKVFQYGD CIALVCADSE ANARAAAEKV 310 320 330 340 350 360 KVDLEELPAY MSGPAAAAED AIEIHPGTPN VYFEQPIVKG EDTGPIFASA DVTVEGDFYV 370 380 390 400 410 420 GRQPHMPIEP DVAFAYMGDD GKCYIHSKSI GVHLHLYMIA PGVGLEPDQL VLVANPMGGT 430 440 450 460 470 480 FGYKFSPTSE ALVAVAAMAT GRPVHLRYNY QQQQQYTGKR SPWEMNVKFA AKKDGTLLAM 490 500 510 520 530 540 ESDWLVDHGP YSEFGDLLTL RGAQFIGAGY NIPNIRGLGR TVATNHVWGS AFRGYGAPQS 550 560 570 580 590 600 MFASECLMDM LAEKLGMDPL ELRYKNAYRP GDTNPTGQEP EVFSLPDMID QLRPKYQAAL 610 620 630 640 650 660 EKAQKESTAT HKKGVGISIG VYGSGLDGPD ASEAWAELNA DGTITVHTAW EDHGQGADIG 670 680 690 700 710 720 CVGTAHEALR PMGVAPEKIK FTWPNTATTP NSGPSGGSRQ QVMTGNAIRV ACENLLKACE 730 740 750 760 770 780 KPGGGYYTYD ELKAADKPTK ITGNWTASGA THCDAVTGLG KPFVVYMYGV FMAEVTVDVA 790 800 810 820 830 840 TGQTTVDGMT LMADLGSLCN QLATDGQIYG GLAQGIGLAL SEDFEDIKKH ATLVGAGFPF 850 860 870 880 890 900 IKQIPDKLDI VYVNHPRPDG PFGASGVGEL PLTSPHAAII NAIKSATGVR IYRLPAYPEK VLEALKA

References

[1]	"Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase." Thoenes U., Flores O.L., Neves A., Devreese B., van Beeumen J.J., Huber R., Romao M.J., Legall J., Moura J.J.G., Rodriges-Pousada C. Eur. J. Biochem. 220:901-910(1994) [PubMed: 8143744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas." Romao M.J., Archer M., Moura I., Moura J.J.G., LeGall J., Engh R., Schneider M., Hof P., Huber R. Science 270:1170-1176(1995) [PubMed: 7502041] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[3]	"A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes." Huber R., Hof P., Duarte R.O., Moura J.J.G., Moura I., Liu M.-Y., LeGall J., Hille R., Archer M., Romao M.J. Proc. Natl. Acad. Sci. U.S.A. 93:8846-8851(1996) [PubMed: 8799115] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]	"Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A." Rebelo J.M., Dias J.M., Huber R., Moura J.J., Romao M.J. J. Biol. Inorg. Chem. 6:791-800(2001) [PubMed: 11713686] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X77222 Genomic DNA. Translation: CAA54439.1.

PIR

A57429.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SIJ	X-ray	2.30	A	1-907	[»]
1VLB	X-ray	1.28	A	1-907	[»]
1ZCS	X-ray	1.45	A	1-907	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.99.7. 7582.

Family and domain databases

InterPro

IPR002888. 2Fe-2S_bd.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
[Graphical view]

Gene3D

G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]

ProDom

PD186071. 2Fe-2S_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MOP_DESGI

Accession

Primary (citable) accession number: Q46509

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 68 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)