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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)DescriptionActionsGraphical viewLength
Metal bindingi40Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi45Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi48Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi60Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi100Iron-sulfur 2 (2Fe-2S)1 Publication1
Metal bindingi103Iron-sulfur 2 (2Fe-2S)1 Publication1
Metal bindingi137Iron-sulfur 2 (2Fe-2S)1 Publication1
Metal bindingi139Iron-sulfur 2 (2Fe-2S)1 Publication1
Metal bindingi653Molybdenum1
Metal bindingi869Molybdenum1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi1.2.99.7. 1907.
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

Pathology & Biotechi

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661021 – 907Aldehyde oxidoreductaseAdd BLAST907

Proteomic databases

PRIDEiQ46509.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1907
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi11 – 17Combined sources7
Helixi23 – 29Combined sources7
Beta strandi39 – 45Combined sources7
Beta strandi49 – 52Combined sources4
Beta strandi55 – 58Combined sources4
Helixi59 – 61Combined sources3
Helixi64 – 66Combined sources3
Beta strandi72 – 74Combined sources3
Helixi76 – 79Combined sources4
Helixi87 – 95Combined sources9
Helixi104 – 117Combined sources14
Helixi123 – 132Combined sources10
Beta strandi138 – 140Combined sources3
Helixi143 – 156Combined sources14
Helixi162 – 165Combined sources4
Helixi185 – 189Combined sources5
Helixi196 – 201Combined sources6
Beta strandi208 – 214Combined sources7
Beta strandi216 – 226Combined sources11
Helixi228 – 231Combined sources4
Beta strandi236 – 240Combined sources5
Helixi242 – 244Combined sources3
Beta strandi249 – 251Combined sources3
Beta strandi267 – 270Combined sources4
Beta strandi272 – 275Combined sources4
Beta strandi281 – 289Combined sources9
Helixi290 – 297Combined sources8
Beta strandi301 – 306Combined sources6
Helixi313 – 317Combined sources5
Beta strandi330 – 341Combined sources12
Helixi343 – 349Combined sources7
Beta strandi351 – 360Combined sources10
Beta strandi372 – 377Combined sources6
Beta strandi383 – 387Combined sources5
Helixi392 – 403Combined sources12
Helixi407 – 409Combined sources3
Beta strandi410 – 414Combined sources5
Helixi423 – 425Combined sources3
Helixi430 – 440Combined sources11
Beta strandi444 – 447Combined sources4
Helixi450 – 455Combined sources6
Beta strandi463 – 471Combined sources9
Beta strandi477 – 487Combined sources11
Helixi495 – 505Combined sources11
Turni506 – 509Combined sources4
Beta strandi514 – 522Combined sources9
Turni533 – 536Combined sources4
Helixi537 – 555Combined sources19
Helixi559 – 566Combined sources8
Helixi585 – 606Combined sources22
Beta strandi609 – 626Combined sources18
Turni627 – 629Combined sources3
Beta strandi631 – 638Combined sources8
Beta strandi644 – 647Combined sources4
Beta strandi653 – 655Combined sources3
Helixi657 – 669Combined sources13
Helixi670 – 672Combined sources3
Helixi676 – 678Combined sources3
Beta strandi679 – 681Combined sources3
Turni686 – 688Combined sources3
Helixi700 – 719Combined sources20
Beta strandi724 – 726Combined sources3
Helixi729 – 734Combined sources6
Beta strandi740 – 746Combined sources7
Turni755 – 757Combined sources3
Beta strandi766 – 778Combined sources13
Turni779 – 781Combined sources3
Beta strandi784 – 794Combined sources11
Helixi801 – 820Combined sources20
Helixi829 – 831Combined sources3
Turni833 – 837Combined sources5
Helixi841 – 843Combined sources3
Beta strandi848 – 852Combined sources5
Beta strandi858 – 860Combined sources3
Helixi861 – 863Combined sources3
Helixi870 – 872Combined sources3
Helixi875 – 887Combined sources13
Beta strandi893 – 895Combined sources3
Helixi898 – 906Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST78

Sequence similaritiesi

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

Family and domain databases

CDDicd00207. fer2. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

Proteomic databases

PRIDEiQ46509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.2.99.7. 1907.
SABIO-RKQ46509.

Miscellaneous databases

EvolutionaryTraceiQ46509.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

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: November 2, 2016
This is version 101 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

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.