Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21631

- SUMT_PSEDE

UniProt

P21631 - SUMT_PSEDE

Protein

Uroporphyrinogen-III C-methyltransferase

Gene

cobA

Organism
Pseudomonas denitrificans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
    Binding sitei130 – 1301S-adenosyl-L-methionine1 Publication
    Binding sitei184 – 1841S-adenosyl-L-methionine; via amide nitrogen1 Publication

    GO - Molecular functioni

    1. precorrin-2 dehydrogenase activity Source: InterPro
    2. uroporphyrin-III C-methyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
    2. siroheme biosynthetic process Source: UniProtKB-UniPathway

    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.
    RETL1328306-WGS:GSTH-2506-MONOMER.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471D → N: Reduces S-adenosyl-L-methionine binding by about 75%. Causes accumulation of precorrin-1. 1 Publication
    Mutagenesisi49 – 491L → A: Reduces S-adenosyl-L-methionine binding by about 50%. Causes slow synthesis of precorrin-2 and accumulation of precorrin-1. 1 Publication
    Mutagenesisi106 – 1061F → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. 1 Publication
    Mutagenesisi130 – 1301T → A: Strongly reduces S-adenosyl-L-methionine binding. Causes slow synthesis of precorrin-2. 1 Publication
    Mutagenesisi183 – 1831Y → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. 1 Publication
    Mutagenesisi184 – 1841M → A: Strongly reduces S-adenosyl-L-methionine binding. Causes drastic effects on enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 280280Uroporphyrinogen-III C-methyltransferasePRO_0000150372Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    280
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 215
    Beta strandi23 – 253
    Beta strandi29 – 313
    Helixi32 – 409
    Beta strandi42 – 465
    Helixi54 – 574
    Beta strandi64 – 663
    Helixi78 – 9013
    Beta strandi95 – 1017
    Beta strandi105 – 1084
    Helixi109 – 1179
    Turni118 – 1203
    Beta strandi123 – 1264
    Turni131 – 1333
    Helixi134 – 1385
    Turni146 – 1483
    Beta strandi150 – 1567
    Helixi170 – 1745
    Beta strandi178 – 1847
    Helixi189 – 19810
    Beta strandi206 – 2127
    Beta strandi219 – 2246
    Turni225 – 2273
    Helixi228 – 2358
    Beta strandi239 – 2468
    Helixi247 – 2515
    Helixi252 – 2554
    Helixi257 – 2615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S4DX-ray2.70A/B/D/E/F/G/H/I/J/K/L/M1-280[»]
    ProteinModelPortaliP21631.
    SMRiP21631. Positions 4-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21631.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 248248Uroporphyrinogen-III C-methyltransferaseAdd
    BLAST
    Regioni100 – 1023S-adenosyl-L-methionine binding

    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

    MIDDLFAGLP ALEKGSVWLV GAGPGDPGLL TLHAANALRQ ADVIVHDALV    50
    NEDCLKLARP GAVLEFAGKR GGKPSPKQRD ISLRLVELAR AGNRVLRLKG 100
    GDPFVFGRGG EEALTLVEHQ VPFRIVPGIT AGIGGLAYAG IPVTHREVNH 150
    AVTFLTGHDS SGLVPDRINW QGIASGSPVI VMYMAMKHIG AITANLIAGG 200
    RSPDEPVAFV CNAATPQQAV LETTLARAEA DVAAAGLEPP AIVVVGEVVR 250
    LRAALDWIGA LDGRKLAADP FANRILRNPA 280
    Length:280
    Mass (Da):29,253
    Last modified:May 1, 1991 - v1
    Checksum:i3D593C535CF0610E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59236 Genomic DNA. Translation: AAA25773.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59236 Genomic DNA. Translation: AAA25773.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S4D X-ray 2.70 A/B/D/E/F/G/H/I/J/K/L/M 1-280 [» ]
    ProteinModelPortali P21631.
    SMRi P21631. Positions 4-270.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00262 ; UER00211 .
    BioCyci MetaCyc:MONOMER-82.
    RETL1328306-WGS:GSTH-2506-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P21631.

    Family and domain databases

    Gene3Di 3.30.950.10. 1 hit.
    3.40.1010.10. 1 hit.
    InterProi IPR000878. 4pyrrol_Mease.
    IPR014777. 4pyrrole_Mease_sub1.
    IPR014776. 4pyrrole_Mease_sub2.
    IPR006366. CobA/CysG_C.
    IPR003043. Uropor_MeTrfase_CS.
    [Graphical view ]
    Pfami PF00590. TP_methylase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53790. SSF53790. 1 hit.
    TIGRFAMsi TIGR01469. cobA_cysG_Cterm. 1 hit.
    PROSITEi PS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a Pseudomonas denitrificans 5.4-kilobase DNA fragment containing five cob genes and identification of structural genes encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase and cobyrinic acid a,c-diamide synthase."
      Crouzet J., Cauchois L., Blanche F., Debussche L., Thibaut D., Rouyez M.-C., Rigault S., Mayaux J.-F., Cameron B.
      J. Bacteriol. 172:5968-5979(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
      Strain: SC510.
    2. "Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans."
      Blanche F., Debussche L., Thibaut D., Crouzet J., Cameron B.
      J. Bacteriol. 171:4222-4231(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    3. "Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis."
      Vevodova J., Graham R.M., Raux E., Schubert H.L., Roper D.I., Brindley A.A., Ian Scott A., Roessner C.A., Stamford N.P.J., Stroupe M.E., Getzoff E.D., Warren M.J., Wilson K.S.
      J. Mol. Biol. 344:419-433(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF APOPROTEIN IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, SUBUNIT, KINETIC PARAMETERS, MUTAGENESIS OF ASP-47; LEU-49; PHE-106; THR-130; TYR-183 AND MET-184.

    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: October 1, 2014
    This is version 79 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