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Protein

Carbon monoxide dehydrogenase medium chain

Gene

coxM

Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
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.2 Publications

Catalytic activityi

CO + a quinone + H2O = CO2 + a quinol.2 Publications

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Kineticsi

  1. KM=16.4 µM for 1,4-benzoquinone1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 365FAD2 Publications
    Nucleotide bindingi111 – 1155FAD2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciOCAR504832:GJPZ-3596-MONOMER.
    BRENDAi1.2.99.2. 4399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbon monoxide dehydrogenase medium chain (EC:1.2.5.32 Publications)
    Short name:
    CO dehydrogenase subunit M
    Short name:
    CO-DH M
    Gene namesi
    Name:coxM
    Ordered Locus Names:OCA5_pHCG300290
    Encoded oniPlasmid megaplasmid pHCG30 Publication
    OrganismiOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
    Taxonomic identifieri504832 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha
    Proteomesi
    • UP000007730 Componenti: Plasmid pHCG3

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Carbon monoxide dehydrogenase medium chainPRO_0000079813Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Helixi14 – 2411Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 336Combined sources
    Helixi37 – 426Combined sources
    Beta strandi49 – 535Combined sources
    Helixi58 – 603Combined sources
    Beta strandi63 – 664Combined sources
    Beta strandi69 – 735Combined sources
    Helixi78 – 836Combined sources
    Helixi85 – 906Combined sources
    Helixi92 – 987Combined sources
    Helixi104 – 1096Combined sources
    Helixi112 – 1176Combined sources
    Helixi125 – 1328Combined sources
    Beta strandi135 – 1406Combined sources
    Beta strandi143 – 1486Combined sources
    Helixi149 – 1524Combined sources
    Beta strandi153 – 1553Combined sources
    Beta strandi158 – 1603Combined sources
    Beta strandi166 – 1738Combined sources
    Beta strandi180 – 1867Combined sources
    Beta strandi195 – 20511Combined sources
    Beta strandi208 – 22215Combined sources
    Helixi227 – 2337Combined sources
    Helixi240 – 25314Combined sources
    Helixi264 – 28522Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N5WX-ray1.50C/F1-288[»]
    1N60X-ray1.19C/F1-288[»]
    1N61X-ray1.30C/F1-288[»]
    1N62X-ray1.09C/F1-288[»]
    1N63X-ray1.21C/F1-288[»]
    1ZXIX-ray1.70C/F1-288[»]
    ProteinModelPortaliP19920.
    SMRiP19920. Positions 1-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19920.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 177177FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK03519.
    OMAiAPFEYER.

    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.

    P19920-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIPGSFDYHR PKSIADAVAL LTKLGEDARP LAGGHSLIPI MKTRLATPEH
    60 70 80 90 100
    LVDLRDIGDL VGIREEGTDV VIGAMTTQHA LIGSDFLAAK LPIIRETSLL
    110 120 130 140 150
    IADPQIRYMG TIGGNAANGD PGNDMPALMQ CLGAAYELTG PEGARIVAAR
    160 170 180 190 200
    DYYQGAYFTA IEPGELLTAI RIPVPPTGHG YAYEKLKRKI GDYATAAAAV
    210 220 230 240 250
    VLTMSGGKCV TASIGLTNVA NTPLWAEEAG KVLVGTALDK PALDKAVALA
    260 270 280
    EAITAPASDG RGPAEYRTKM AGVMLRRAVE RAKARAKN
    Length:288
    Mass (Da):30,241
    Last modified:July 11, 2002 - v2
    Checksum:iE3EA980056731FC5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → MM AA sequence (PubMed:2818128).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002827 Genomic DNA. Translation: AEI08104.1.
    PIRiA56279.
    RefSeqiWP_013913728.1. NC_015689.1.

    Genome annotation databases

    EnsemblBacteriaiAEI08104; AEI08104; OCA5_pHCG300290.
    KEGGiocg:OCA5_pHCG300290.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002827 Genomic DNA. Translation: AEI08104.1.
    PIRiA56279.
    RefSeqiWP_013913728.1. NC_015689.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N5WX-ray1.50C/F1-288[»]
    1N60X-ray1.19C/F1-288[»]
    1N61X-ray1.30C/F1-288[»]
    1N62X-ray1.09C/F1-288[»]
    1N63X-ray1.21C/F1-288[»]
    1ZXIX-ray1.70C/F1-288[»]
    ProteinModelPortaliP19920.
    SMRiP19920. Positions 1-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAEI08104; AEI08104; OCA5_pHCG300290.
    KEGGiocg:OCA5_pHCG300290.

    Phylogenomic databases

    KOiK03519.
    OMAiAPFEYER.

    Enzyme and pathway databases

    BioCyciOCAR504832:GJPZ-3596-MONOMER.
    BRENDAi1.2.99.2. 4399.

    Miscellaneous databases

    EvolutionaryTraceiP19920.

    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_OLICO
    AccessioniPrimary (citable) accession number: P19920
    Secondary accession number(s): F8C0Z4, Q51323
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 11, 2002
    Last modified: September 7, 2016
    This is version 111 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, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

    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.