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Protein

Aldehyde oxidoreductase

Gene

mop

Organism
Desulfovibrio gigas
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi45 – 451Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi60 – 601Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi103 – 1031Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi137 – 1371Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi653 – 6531Molybdenum
Metal bindingi869 – 8691Molybdenum

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. aldehyde dehydrogenase (FAD-independent) activity Source: UniProtKB-EC
  3. electron carrier activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

SABIO-RKQ46509.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidoreductase (EC:1.2.99.7)
Alternative name(s):
Molybdenum iron sulfur protein
Gene namesi
Name:mop
OrganismiDesulfovibrio gigas
Taxonomic identifieri879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 907907Aldehyde oxidoreductasePRO_0000166102Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
907
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi11 – 177Combined sources
Helixi23 – 297Combined sources
Beta strandi39 – 457Combined sources
Beta strandi49 – 524Combined sources
Beta strandi55 – 584Combined sources
Helixi59 – 613Combined sources
Helixi64 – 663Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 794Combined sources
Helixi87 – 959Combined sources
Helixi104 – 11714Combined sources
Helixi123 – 13210Combined sources
Beta strandi138 – 1403Combined sources
Helixi143 – 15614Combined sources
Helixi162 – 1654Combined sources
Helixi185 – 1895Combined sources
Helixi196 – 2016Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi216 – 22611Combined sources
Helixi228 – 2314Combined sources
Beta strandi236 – 2405Combined sources
Helixi242 – 2443Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi281 – 2899Combined sources
Helixi290 – 2978Combined sources
Beta strandi301 – 3066Combined sources
Helixi313 – 3175Combined sources
Beta strandi330 – 34112Combined sources
Helixi343 – 3497Combined sources
Beta strandi351 – 36010Combined sources
Beta strandi372 – 3776Combined sources
Beta strandi383 – 3875Combined sources
Helixi392 – 40312Combined sources
Helixi407 – 4093Combined sources
Beta strandi410 – 4145Combined sources
Helixi423 – 4253Combined sources
Helixi430 – 44011Combined sources
Beta strandi444 – 4474Combined sources
Helixi450 – 4556Combined sources
Beta strandi463 – 4719Combined sources
Beta strandi477 – 48711Combined sources
Helixi495 – 50511Combined sources
Turni506 – 5094Combined sources
Beta strandi514 – 5229Combined sources
Turni533 – 5364Combined sources
Helixi537 – 55519Combined sources
Helixi559 – 5668Combined sources
Helixi585 – 60622Combined sources
Beta strandi609 – 62618Combined sources
Turni627 – 6293Combined sources
Beta strandi631 – 6388Combined sources
Beta strandi644 – 6474Combined sources
Beta strandi653 – 6553Combined sources
Helixi657 – 66913Combined sources
Helixi670 – 6723Combined sources
Helixi676 – 6783Combined sources
Beta strandi679 – 6813Combined sources
Turni686 – 6883Combined sources
Helixi700 – 71920Combined sources
Beta strandi724 – 7263Combined sources
Helixi729 – 7346Combined sources
Beta strandi740 – 7467Combined sources
Turni755 – 7573Combined sources
Beta strandi766 – 77813Combined sources
Turni779 – 7813Combined sources
Beta strandi784 – 79411Combined sources
Helixi801 – 82020Combined sources
Helixi829 – 8313Combined sources
Turni833 – 8375Combined sources
Helixi841 – 8433Combined sources
Beta strandi848 – 8525Combined sources
Beta strandi858 – 8603Combined sources
Helixi861 – 8633Combined sources
Helixi870 – 8723Combined sources
Helixi875 – 88713Combined sources
Beta strandi893 – 8953Combined sources
Helixi898 – 9069Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SIJX-ray2.30A1-907[»]
1VLBX-ray1.28A1-907[»]
3FAHX-ray1.72A1-907[»]
3FC4X-ray1.79A1-907[»]
3L4PX-ray1.45A1-907[»]
4C7YX-ray1.57A1-907[»]
4C7ZX-ray1.55A1-907[»]
4C80X-ray1.50A1-907[»]
4US8X-ray1.49A1-907[»]
4US9X-ray1.40A1-907[»]
4USAX-ray1.13A1-907[»]
ProteinModelPortaliQ46509.
SMRiQ46509. Positions 1-907.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 79782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46509-1 [UniParc]FASTAAdd to basket

« Hide

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

VLEALKA
Length:907
Mass (Da):97,035
Last modified:November 1, 1996 - v1
Checksum:i898E7EEF708A64DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77222 Genomic DNA. Translation: CAA54439.1.
PIRiA57429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77222 Genomic DNA. Translation: CAA54439.1.
PIRiA57429.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SIJX-ray2.30A1-907[»]
1VLBX-ray1.28A1-907[»]
3FAHX-ray1.72A1-907[»]
3FC4X-ray1.79A1-907[»]
3L4PX-ray1.45A1-907[»]
4C7YX-ray1.57A1-907[»]
4C7ZX-ray1.55A1-907[»]
4C80X-ray1.50A1-907[»]
4US8X-ray1.49A1-907[»]
4US9X-ray1.40A1-907[»]
4USAX-ray1.13A1-907[»]
ProteinModelPortaliQ46509.
SMRiQ46509. Positions 1-907.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ46509.

Miscellaneous databases

EvolutionaryTraceiQ46509.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).

Entry informationi

Entry nameiMOP_DESGI
AccessioniPrimary (citable) accession number: Q46509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 92 of the entry and version 1 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

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 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.