UniProtKB - Q46509 (MOP_DESGI)

BLAST

>sp|Q46509|MOP_DESGI Aldehyde oxidoreductase OS=Desulfovibrio gigas OX=879 GN=mop PE=1 SV=1
MIQKVITVNGIEQNLFVDAEALLSDVLRQQLGLTGVKVGCEQGQCGACSVILDGKVVRAC
VTKMKRVADGAQITTIEGVGQPENLHPLQKAWVLHGGAQCGFCSPGFIVSAKGLLDTNAD
PSREDVRDWFQKHRNACRCTGYKPLVDAVMDAAAVINGKKPETDLEFKMPADGRIWGSKY
PRPTAVAKVTGTLDYGADLGLKMPAGTLHLAMVQAKVSHANIKGIDTSEALTMPGVHSVI
THKDVKGKNRITGLITFPTNKGDGWDRPILCDEKVFQYGDCIALVCADSEANARAAAEKV
KVDLEELPAYMSGPAAAAEDAIEIHPGTPNVYFEQPIVKGEDTGPIFASADVTVEGDFYV
GRQPHMPIEPDVAFAYMGDDGKCYIHSKSIGVHLHLYMIAPGVGLEPDQLVLVANPMGGT
FGYKFSPTSEALVAVAAMATGRPVHLRYNYQQQQQYTGKRSPWEMNVKFAAKKDGTLLAM
ESDWLVDHGPYSEFGDLLTLRGAQFIGAGYNIPNIRGLGRTVATNHVWGSAFRGYGAPQS
MFASECLMDMLAEKLGMDPLELRYKNAYRPGDTNPTGQEPEVFSLPDMIDQLRPKYQAAL
EKAQKESTATHKKGVGISIGVYGSGLDGPDASEAWAELNADGTITVHTAWEDHGQGADIG
CVGTAHEALRPMGVAPEKIKFTWPNTATTPNSGPSGGSRQQVMTGNAIRVACENLLKACE
KPGGGYYTYDELKAADKPTKITGNWTASGATHCDAVTGLGKPFVVYMYGVFMAEVTVDVA
TGQTTVDGMTLMADLGSLCNQLATDGQIYGGLAQGIGLALSEDFEDIKKHATLVGAGFPF
IKQIPDKLDIVYVNHPRPDGPFGASGVGELPLTSPHAAIINAIKSATGVRIYRLPAYPEK
VLEALKA

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History
Entry version 109 (28 Mar 2018)
Sequence version 1 (01 Nov 1996)
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Protein

Aldehyde oxidoreductase

Gene

mop

Organism

Desulfovibrio gigas

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalytic activityⁱ

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

Cofactorⁱ

Protein has several cofactor binding sites:

Mo-molybdopterin cytosine dinucleotideNote: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.
[2Fe-2S] clusterNote: Binds 2 [2Fe-2S] clusters per subunit.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	40	Iron-sulfur 1 (2Fe-2S)1 Publication	1
Metal bindingⁱ	45	Iron-sulfur 1 (2Fe-2S)1 Publication	1
Metal bindingⁱ	48	Iron-sulfur 1 (2Fe-2S)1 Publication	1
Metal bindingⁱ	60	Iron-sulfur 1 (2Fe-2S)1 Publication	1
Metal bindingⁱ	100	Iron-sulfur 2 (2Fe-2S)1 Publication	1
Metal bindingⁱ	103	Iron-sulfur 2 (2Fe-2S)1 Publication	1
Metal bindingⁱ	137	Iron-sulfur 2 (2Fe-2S)1 Publication	1
Metal bindingⁱ	139	Iron-sulfur 2 (2Fe-2S)1 Publication	1
Metal bindingⁱ	653	Molybdenum	1
Metal bindingⁱ	869	Molybdenum	1

GO - Molecular functionⁱ

2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
aldehyde dehydrogenase (FAD-independent) activity Source: UniProtKB-EC
electron transfer activity Source: InterPro
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BRENDAⁱ	1.2.99.7 1907
SABIO-RKⁱ	Q46509

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Aldehyde oxidoreductase (EC:1.2.99.7) Alternative name(s): Molybdenum iron sulfur protein
Gene namesⁱ	Name:mop
Organismⁱ	Desulfovibrio gigas
Taxonomic identifierⁱ	879 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02325 Isopropyl Alcohol DB02137 Molybdenum Cofactor

DrugBankⁱ

DB02325 Isopropyl Alcohol
DB02137 Molybdenum Cofactor

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000166102	1 – 907	Aldehyde oxidoreductaseAdd BLAST		907

Proteomic databases

PRIDEⁱ	Q46509

PRIDEⁱ

Q46509

Interactionⁱ

Subunit structureⁱ

Homodimer.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 8	Combined sources	7
Beta strandⁱ	11 – 17	Combined sources	7
Helixⁱ	23 – 29	Combined sources	7
Beta strandⁱ	39 – 45	Combined sources	7
Beta strandⁱ	49 – 52	Combined sources	4
Beta strandⁱ	55 – 58	Combined sources	4
Helixⁱ	59 – 61	Combined sources	3
Helixⁱ	64 – 66	Combined sources	3
Beta strandⁱ	72 – 74	Combined sources	3
Helixⁱ	76 – 79	Combined sources	4
Helixⁱ	87 – 95	Combined sources	9
Helixⁱ	104 – 117	Combined sources	14
Helixⁱ	123 – 132	Combined sources	10
Beta strandⁱ	138 – 140	Combined sources	3
Helixⁱ	143 – 156	Combined sources	14
Helixⁱ	162 – 165	Combined sources	4
Helixⁱ	185 – 189	Combined sources	5
Helixⁱ	196 – 201	Combined sources	6
Beta strandⁱ	208 – 214	Combined sources	7
Beta strandⁱ	216 – 226	Combined sources	11
Helixⁱ	228 – 231	Combined sources	4
Beta strandⁱ	236 – 240	Combined sources	5
Helixⁱ	242 – 244	Combined sources	3
Beta strandⁱ	249 – 251	Combined sources	3
Beta strandⁱ	267 – 270	Combined sources	4
Beta strandⁱ	272 – 275	Combined sources	4
Beta strandⁱ	281 – 289	Combined sources	9
Helixⁱ	290 – 297	Combined sources	8
Beta strandⁱ	301 – 306	Combined sources	6
Helixⁱ	313 – 317	Combined sources	5
Beta strandⁱ	330 – 341	Combined sources	12
Helixⁱ	343 – 349	Combined sources	7
Beta strandⁱ	351 – 360	Combined sources	10
Beta strandⁱ	372 – 377	Combined sources	6
Beta strandⁱ	383 – 387	Combined sources	5
Helixⁱ	392 – 403	Combined sources	12
Helixⁱ	407 – 409	Combined sources	3
Beta strandⁱ	410 – 414	Combined sources	5
Helixⁱ	423 – 425	Combined sources	3
Helixⁱ	430 – 440	Combined sources	11
Beta strandⁱ	444 – 447	Combined sources	4
Helixⁱ	450 – 455	Combined sources	6
Beta strandⁱ	463 – 471	Combined sources	9
Beta strandⁱ	477 – 487	Combined sources	11
Helixⁱ	495 – 505	Combined sources	11
Turnⁱ	506 – 509	Combined sources	4
Beta strandⁱ	514 – 522	Combined sources	9
Turnⁱ	533 – 536	Combined sources	4
Helixⁱ	537 – 555	Combined sources	19
Helixⁱ	559 – 566	Combined sources	8
Helixⁱ	585 – 606	Combined sources	22
Beta strandⁱ	609 – 626	Combined sources	18
Turnⁱ	627 – 629	Combined sources	3
Beta strandⁱ	631 – 638	Combined sources	8
Beta strandⁱ	644 – 647	Combined sources	4
Beta strandⁱ	653 – 655	Combined sources	3
Helixⁱ	657 – 669	Combined sources	13
Helixⁱ	670 – 672	Combined sources	3
Helixⁱ	676 – 678	Combined sources	3
Beta strandⁱ	679 – 681	Combined sources	3
Turnⁱ	686 – 688	Combined sources	3
Helixⁱ	700 – 719	Combined sources	20
Beta strandⁱ	724 – 726	Combined sources	3
Helixⁱ	729 – 734	Combined sources	6
Beta strandⁱ	740 – 746	Combined sources	7
Turnⁱ	755 – 757	Combined sources	3
Beta strandⁱ	766 – 778	Combined sources	13
Turnⁱ	779 – 781	Combined sources	3
Beta strandⁱ	784 – 794	Combined sources	11
Helixⁱ	801 – 820	Combined sources	20
Helixⁱ	829 – 831	Combined sources	3
Turnⁱ	833 – 837	Combined sources	5
Helixⁱ	841 – 843	Combined sources	3
Beta strandⁱ	848 – 852	Combined sources	5
Beta strandⁱ	858 – 860	Combined sources	3
Helixⁱ	861 – 863	Combined sources	3
Helixⁱ	870 – 872	Combined sources	3
Helixⁱ	875 – 887	Combined sources	13
Beta strandⁱ	893 – 895	Combined sources	3
Helixⁱ	898 – 906	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	Q46509
SMRⁱ	Q46509
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q46509

EvolutionaryTraceⁱ

Q46509

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 79	2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST		78

Sequence similaritiesⁱ

Belongs to the xanthine dehydrogenase family.Curated

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00207 fer2, 1 hit
Gene3Dⁱ	3.10.20.30, 1 hit
InterProⁱ	View protein in InterPro IPR002888 2Fe-2S-bd IPR036884 2Fe-2S-bd_dom_sf IPR036010 2Fe-2S_ferredoxin-like_sf IPR001041 2Fe-2S_ferredoxin-type IPR006058 2Fe2S_fd_BS IPR000674 Ald_Oxase/Xan_DH_a/b IPR036856 Ald_Oxase/Xan_DH_a/b_sf IPR008274 AldOxase/xan_DH_Mopterin-bd IPR037165 AldOxase/xan_DH_Mopterin-bd_sf IPR012675 Beta-grasp_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01315 Ald_Xan_dh_C, 1 hit PF02738 Ald_Xan_dh_C2, 1 hit PF00111 Fer2, 1 hit PF01799 Fer2_2, 1 hit
SMARTⁱ	View protein in SMART SM01008 Ald_Xan_dh_C, 1 hit
SUPFAMⁱ	SSF47741 SSF47741, 1 hit SSF54292 SSF54292, 1 hit SSF54665 SSF54665, 1 hit SSF56003 SSF56003, 1 hit
PROSITEⁱ	View protein in PROSITE PS00197 2FE2S_FER_1, 1 hit PS51085 2FE2S_FER_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q46509-1 [UniParc]FASTA Add 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

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X77222 Genomic DNA Translation: CAA54439.1
PIRⁱ	A57429

Protein	Similar proteins		Species	Score	Length	Source
Q46509	Aldehyde oxidoreductase		DESGG		907	UniRef100_Q46509

Protein	Similar proteins		Species	Score	Length	Source
Q46509	Aldehyde oxidoreductase		DESGG		907	UniRef90_Q46509

Protein	Similar proteins		Species	Score	Length	Source
Q46509	Aldehyde oxidoreductase		DESGG		907	UniRef50_Q46509
Aldehyde oxidoreductase		Blautia sp. YL58		912
Aldehyde dehydrogenase, molybdenum-binding subunit apoprotein		Desulfosporosinus lacus DSM 15449		908
Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL-like protein		Synergistales bacterium 57_84		939
Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL-like protein		Synergistales bacterium 58_81		939
+158

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X77222 Genomic DNA Translation: CAA54439.1
PIRⁱ	A57429

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1SIJ	X-ray	2.30	A	1-907	[»]
	1VLB	X-ray	1.28	A	1-907	[»]
	3FAH	X-ray	1.72	A	1-907	[»]
	3FC4	X-ray	1.79	A	1-907	[»]
	3L4P	X-ray	1.45	A	1-907	[»]
	4C7Y	X-ray	1.57	A	1-907	[»]
	4C7Z	X-ray	1.55	A	1-907	[»]
	4C80	X-ray	1.50	A	1-907	[»]
	4US8	X-ray	1.49	A	1-907	[»]
	4US9	X-ray	1.40	A	1-907	[»]
	4USA	X-ray	1.13	A	1-907	[»]
ProteinModelPortalⁱ	Q46509
SMRⁱ	Q46509
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Chemistry databases

DrugBankⁱ	DB02325 Isopropyl Alcohol DB02137 Molybdenum Cofactor

DrugBankⁱ

DB02325 Isopropyl Alcohol
DB02137 Molybdenum Cofactor

Proteomic databases

PRIDEⁱ	Q46509

PRIDEⁱ

Q46509

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

BRENDAⁱ	1.2.99.7 1907
SABIO-RKⁱ	Q46509

Miscellaneous databases

EvolutionaryTraceⁱ	Q46509

EvolutionaryTraceⁱ

Q46509

Family and domain databases

CDDⁱ	cd00207 fer2, 1 hit
Gene3Dⁱ	3.10.20.30, 1 hit
InterProⁱ	View protein in InterPro IPR002888 2Fe-2S-bd IPR036884 2Fe-2S-bd_dom_sf IPR036010 2Fe-2S_ferredoxin-like_sf IPR001041 2Fe-2S_ferredoxin-type IPR006058 2Fe2S_fd_BS IPR000674 Ald_Oxase/Xan_DH_a/b IPR036856 Ald_Oxase/Xan_DH_a/b_sf IPR008274 AldOxase/xan_DH_Mopterin-bd IPR037165 AldOxase/xan_DH_Mopterin-bd_sf IPR012675 Beta-grasp_dom_sf
Pfamⁱ	View protein in Pfam PF01315 Ald_Xan_dh_C, 1 hit PF02738 Ald_Xan_dh_C2, 1 hit PF00111 Fer2, 1 hit PF01799 Fer2_2, 1 hit
SMARTⁱ	View protein in SMART SM01008 Ald_Xan_dh_C, 1 hit
SUPFAMⁱ	SSF47741 SSF47741, 1 hit SSF54292 SSF54292, 1 hit SSF54665 SSF54665, 1 hit SSF56003 SSF56003, 1 hit
PROSITEⁱ	View protein in PROSITE PS00197 2FE2S_FER_1, 1 hit PS51085 2FE2S_FER_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MOP_DESGI
Accessionⁱ	Q46509Primary (citable) accession number: Q46509
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	November 1, 1996
	Last modified:	March 28, 2018
	This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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Aldehyde oxidoreductase

mop

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ