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P21638

- COBH_PSEDE

UniProt

P21638 - COBH_PSEDE

Protein

Precorrin-8X methylmutase

Gene

cobH

Organism
Pseudomonas denitrificans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.1 Publication

    Catalytic activityi

    Precorrin-8X = hydrogenobyrinate.1 Publication

    Kineticsi

    1. KM=0.91 µM for precorrin-8X1 Publication

    Vmax=230 nmol/h/mg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei17 – 171Substrate
    Binding sitei40 – 401Substrate
    Active sitei43 – 431Proton donor/acceptor1 Publication

    GO - Molecular functioni

    1. precorrin-8X methylmutase activity Source: InterPro

    GO - Biological processi

    1. cobalamin biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Cobalamin biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-115.
    RETL1328306-WGS:GSTH-6323-MONOMER.
    UniPathwayiUPA00148; UER00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Precorrin-8X methylmutase (EC:5.4.99.61)
    Alternative name(s):
    HBA synthase
    Precorrin isomerase
    Gene namesi
    Name:cobH
    OrganismiPseudomonas denitrificans
    Taxonomic identifieri43306 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 210209Precorrin-8X methylmutasePRO_0000135926Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2415
    Beta strandi28 – 303
    Helixi32 – 4514
    Helixi48 – 536
    Beta strandi54 – 563
    Helixi60 – 6910
    Beta strandi74 – 785
    Helixi79 – 846
    Helixi87 – 893
    Beta strandi96 – 983
    Helixi104 – 1129
    Helixi116 – 1194
    Helixi120 – 1245
    Helixi125 – 1284
    Beta strandi132 – 1354
    Helixi139 – 15012
    Beta strandi157 – 1615
    Beta strandi165 – 1684
    Helixi169 – 17810
    Beta strandi185 – 1884
    Helixi195 – 20612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F2VX-ray2.10A2-210[»]
    1I1HX-ray2.60A2-210[»]
    ProteinModelPortaliP21638.
    SMRiP21638. Positions 2-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21638.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CobH/CbiC family.Curated

    Family and domain databases

    Gene3Di3.40.50.10230. 1 hit.
    InterProiIPR003722. Cbl_synth_CobH/CbiC.
    [Graphical view]
    PfamiPF02570. CbiC. 1 hit.
    [Graphical view]
    SUPFAMiSSF63965. SSF63965. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21638-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEYDYIRDG NAIYERSFAI IRAEADLSRF SEEEADLAVR MVHACGSVEA    50
    TRQFVFSPDF VSSARAALKA GAPILCDAEM VAHGVTRARL PAGNEVICTL 100
    RDPRTPALAA EIGNTRSAAA LKLWSERLAG SVVAIGNAPT ALFFLLEMLR 150
    DGAPKPAAIL GMPVGFVGAA ESKDALAENS YGVPFAIVRG RLGGSAMTAA 200
    ALNSLARPGL 210
    Length:210
    Mass (Da):22,064
    Last modified:May 1, 1991 - v1
    Checksum:i506D1C4C5D972B3F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59301 Genomic DNA. Translation: AAA25796.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59301 Genomic DNA. Translation: AAA25796.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F2V X-ray 2.10 A 2-210 [» ]
    1I1H X-ray 2.60 A 2-210 [» ]
    ProteinModelPortali P21638.
    SMRi P21638. Positions 2-210.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00219 .
    BioCyci MetaCyc:MONOMER-115.
    RETL1328306-WGS:GSTH-6323-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P21638.

    Family and domain databases

    Gene3Di 3.40.50.10230. 1 hit.
    InterProi IPR003722. Cbl_synth_CobH/CbiC.
    [Graphical view ]
    Pfami PF02570. CbiC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63965. SSF63965. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid."
      Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F., Thibaut D., Debussche L.
      J. Bacteriol. 172:5980-5990(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SC510.
    2. "The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate."
      Thibaut D., Couder M., Famechon A., Debussche L., Cameron B., Crouzet J., Blanche F.
      J. Bacteriol. 174:1043-1049(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-210 OF APOENZYME AND IN COMPLEX WITH HYDROGENOBYRINATE, SUBUNIT, ACTIVE SITE, REACTION MECHANISM.

    Entry informationi

    Entry nameiCOBH_PSEDE
    AccessioniPrimary (citable) accession number: P21638
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 80 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, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3