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Protein

Carbon monoxide dehydrogenase medium chain

Gene

cutM

Organism
Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of carbon monoxide to carbon dioxide.By similarity

Catalytic activityi

CO + a quinone + H2O = CO2 + a quinol.By similarity

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 36FAD5
Nucleotide bindingi111 – 115FAD5

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase medium chain (EC:1.2.5.3By similarity)
Short name:
CO dehydrogenase subunit M
Short name:
CO-DH M
Gene namesi
Name:cutM
OrganismiHydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Taxonomic identifieri47421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeHydrogenophaga

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798121 – 287Carbon monoxide dehydrogenase medium chainAdd BLAST287

Interactioni

Subunit structurei

Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.1 Publication

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Helixi14 – 24Combined sources11
Helixi25 – 27Combined sources3
Beta strandi28 – 33Combined sources6
Helixi37 – 42Combined sources6
Beta strandi49 – 53Combined sources5
Helixi58 – 60Combined sources3
Beta strandi63 – 66Combined sources4
Beta strandi69 – 73Combined sources5
Helixi78 – 83Combined sources6
Helixi85 – 90Combined sources6
Helixi92 – 97Combined sources6
Helixi98 – 100Combined sources3
Helixi106 – 108Combined sources3
Helixi112 – 117Combined sources6
Helixi125 – 131Combined sources7
Beta strandi135 – 140Combined sources6
Beta strandi143 – 149Combined sources7
Beta strandi153 – 155Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi166 – 173Combined sources8
Beta strandi180 – 186Combined sources7
Beta strandi195 – 205Combined sources11
Beta strandi208 – 222Combined sources15
Helixi227 – 231Combined sources5
Helixi240 – 252Combined sources13
Helixi264 – 285Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35C/F1-287[»]
1FFVX-ray2.25C/F1-287[»]
ProteinModelPortaliP19914.
SMRiP19914.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 177FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST177

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPPRFEYHA PKSVGEAVAL LGQLGSDAKL LAGGHSLLPM MKLRFAQPEH
60 70 80 90 100
LIDINRIPEL RGIREEGSTV VIGAMTVEND LISSPIVQAR LPLLAEAAKL
110 120 130 140 150
IADPQVRNRG TIGGDIAHGH PGNDHPALSI AVEAHFVLEG PNGRRTVPAD
160 170 180 190 200
GFFLGTYMTL LEENEVMVEI RVPAFAQGTG WAYEKLKRKT GDWATAGCAV
210 220 230 240 250
VMRKSGNTVS HIRIALTNVA PTALRREGGR SRLLGKAFTK EAVQAAADAA
260 270 280
IAICEPAEDL RGDADYKTAM AGQMVKRALN AAWARCA
Length:287
Mass (Da):30,722
Last modified:July 11, 2002 - v2
Checksum:iF3E9848BDCF4138E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 3IP → MI AA sequence (PubMed:2818128).Curated2
Sequence conflicti13S → H AA sequence (PubMed:2818128).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00361.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00361.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35C/F1-287[»]
1FFVX-ray2.25C/F1-287[»]
ProteinModelPortaliP19914.
SMRiP19914.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19914.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCMM_HYDPS
AccessioniPrimary (citable) accession number: P19914
Secondary accession number(s): Q9ZAR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: November 2, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.