Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Uroporphyrinogen-III C-methyltransferase

Gene

cobA

Organism
Pseudomonas denitrificans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the methylation of both C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin.

Catalytic activityi

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.

Kineticsi

  1. KM=6.3 µM for S-adenosyl-L-methionine1 Publication
  2. KM=1.0 µM for uroporphyrinogen III1 Publication

    Pathwayi: adenosylcobalamin biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.
    Proteins known to be involved in this subpathway in this organism are:
    1. Uroporphyrinogen-III C-methyltransferase (cobA)
    This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

    Pathwayi: siroheme biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.
    Proteins known to be involved in this subpathway in this organism are:
    1. Uroporphyrinogen-III C-methyltransferase (cobA)
    This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei24S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
    Binding sitei130S-adenosyl-L-methionine1 Publication1
    Binding sitei184S-adenosyl-L-methionine; via amide nitrogen1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Cobalamin biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-82.
    UniPathwayiUPA00148; UER00211.
    UPA00262; UER00211.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uroporphyrinogen-III C-methyltransferase (EC:2.1.1.107)
    Short name:
    Urogen III methylase
    Alternative name(s):
    SUMT
    Uroporphyrinogen III methylase
    Short name:
    UROM
    Gene namesi
    Name:cobA
    OrganismiPseudomonas denitrificans
    Taxonomic identifieri43306 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi47D → N: Reduces S-adenosyl-L-methionine binding by about 75%. Causes accumulation of precorrin-1. 1 Publication1
    Mutagenesisi49L → A: Reduces S-adenosyl-L-methionine binding by about 50%. Causes slow synthesis of precorrin-2 and accumulation of precorrin-1. 1 Publication1
    Mutagenesisi106F → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. 1 Publication1
    Mutagenesisi130T → A: Strongly reduces S-adenosyl-L-methionine binding. Causes slow synthesis of precorrin-2. 1 Publication1
    Mutagenesisi183Y → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. 1 Publication1
    Mutagenesisi184M → A: Strongly reduces S-adenosyl-L-methionine binding. Causes drastic effects on enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001503721 – 280Uroporphyrinogen-III C-methyltransferaseAdd BLAST280

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1280
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi17 – 21Combined sources5
    Beta strandi23 – 25Combined sources3
    Beta strandi29 – 31Combined sources3
    Helixi32 – 40Combined sources9
    Beta strandi42 – 46Combined sources5
    Helixi54 – 57Combined sources4
    Beta strandi64 – 66Combined sources3
    Helixi78 – 90Combined sources13
    Beta strandi95 – 101Combined sources7
    Beta strandi105 – 108Combined sources4
    Helixi109 – 117Combined sources9
    Turni118 – 120Combined sources3
    Beta strandi123 – 126Combined sources4
    Turni131 – 133Combined sources3
    Helixi134 – 138Combined sources5
    Turni146 – 148Combined sources3
    Beta strandi150 – 156Combined sources7
    Helixi170 – 174Combined sources5
    Beta strandi178 – 184Combined sources7
    Helixi189 – 198Combined sources10
    Beta strandi206 – 212Combined sources7
    Beta strandi219 – 224Combined sources6
    Turni225 – 227Combined sources3
    Helixi228 – 235Combined sources8
    Beta strandi239 – 246Combined sources8
    Helixi247 – 251Combined sources5
    Helixi252 – 255Combined sources4
    Helixi257 – 261Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1S4DX-ray2.70A/B/D/E/F/G/H/I/J/K/L/M1-280[»]
    ProteinModelPortaliP21631.
    SMRiP21631.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21631.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 248Uroporphyrinogen-III C-methyltransferaseAdd BLAST248
    Regioni100 – 102S-adenosyl-L-methionine binding3

    Sequence similaritiesi

    Belongs to the precorrin methyltransferase family.Curated

    Family and domain databases

    Gene3Di3.30.950.10. 1 hit.
    3.40.1010.10. 1 hit.
    InterProiIPR000878. 4pyrrol_Mease.
    IPR014777. 4pyrrole_Mease_sub1.
    IPR014776. 4pyrrole_Mease_sub2.
    IPR006366. CobA/CysG_C.
    IPR003043. Uropor_MeTrfase_CS.
    [Graphical view]
    PfamiPF00590. TP_methylase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53790. SSF53790. 1 hit.
    TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
    PROSITEiPS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21631-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIDDLFAGLP ALEKGSVWLV GAGPGDPGLL TLHAANALRQ ADVIVHDALV
    60 70 80 90 100
    NEDCLKLARP GAVLEFAGKR GGKPSPKQRD ISLRLVELAR AGNRVLRLKG
    110 120 130 140 150
    GDPFVFGRGG EEALTLVEHQ VPFRIVPGIT AGIGGLAYAG IPVTHREVNH
    160 170 180 190 200
    AVTFLTGHDS SGLVPDRINW QGIASGSPVI VMYMAMKHIG AITANLIAGG
    210 220 230 240 250
    RSPDEPVAFV CNAATPQQAV LETTLARAEA DVAAAGLEPP AIVVVGEVVR
    260 270 280
    LRAALDWIGA LDGRKLAADP FANRILRNPA
    Length:280
    Mass (Da):29,253
    Last modified:May 1, 1991 - v1
    Checksum:i3D593C535CF0610E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59236 Genomic DNA. Translation: AAA25773.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59236 Genomic DNA. Translation: AAA25773.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1S4DX-ray2.70A/B/D/E/F/G/H/I/J/K/L/M1-280[»]
    ProteinModelPortaliP21631.
    SMRiP21631.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00148; UER00211.
    UPA00262; UER00211.
    BioCyciMetaCyc:MONOMER-82.

    Miscellaneous databases

    EvolutionaryTraceiP21631.

    Family and domain databases

    Gene3Di3.30.950.10. 1 hit.
    3.40.1010.10. 1 hit.
    InterProiIPR000878. 4pyrrol_Mease.
    IPR014777. 4pyrrole_Mease_sub1.
    IPR014776. 4pyrrole_Mease_sub2.
    IPR006366. CobA/CysG_C.
    IPR003043. Uropor_MeTrfase_CS.
    [Graphical view]
    PfamiPF00590. TP_methylase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53790. SSF53790. 1 hit.
    TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
    PROSITEiPS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSUMT_PSEDE
    AccessioniPrimary (citable) accession number: P21631
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: November 2, 2016
    This is version 85 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

    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.