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Q55749 (SUMT_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uroporphyrinogen-III C-methyltransferase

Short name=Urogen III methylase
EC=2.1.1.107
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name=UROM
Gene names
Name:cobA
Ordered Locus Names:sll0378
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes both methylations at 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 By similarity.

Catalytic activity

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

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

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.

Sequence similarities

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Uroporphyrinogen-III C-methyltransferase
PRO_0000150375

Regions

Region96 – 983S-adenosyl-L-methionine binding By similarity

Sites

Binding site201S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1261S-adenosyl-L-methionine By similarity
Binding site1801S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55749 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 581847CFF32C7BDE

FASTA26327,833
        10         20         30         40         50         60 
MVVRLQNGLM GKVYLVGAGP GDPGLITVKG KTLLENAEAV VYDALVSTAI LAMVNPQAEL 

        70         80         90        100        110        120 
IDAGKRRGRH TKLQSETTQL LAQLAEKHAV VVRLKGGDPF IFGRGGEEME DLVKAGIEVE 

       130        140        150        160        170        180 
VVPGITAGIA APAYAQIPLT HRAYSSSVTF VTGHESAGKY RPEVNWAAIA KGSETIVIYM 

       190        200        210        220        230        240 
GVYSLATILP QLMLAGLGED TPIALIRWGT CPEQQKLVGT FATILAQIEV ENFQAPAIVV 

       250        260 
IGAVVNYPAN LRQQLAPILG GVN 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10394.1.
PIRS76548.
RefSeqNP_442324.1. NC_000911.1.
YP_005652384.1. NC_017277.1.
YP_007452200.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.sll0378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10394; BAA10394; BAA10394.
GeneID952490.
KEGGsyn:sll0378.
syy:SYNGTS_2431.
syz:MYO_124560.
PATRIC23842312. VBISynSp132158_2696.

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290519.
KOK02303.
OMACQNDISL.
OrthoDBEOG6DRPFR.
PhylomeDBQ55749.

Enzyme and pathway databases

UniPathwayUPA00148; UER00211.
UPA00262; UER00211.

Family and domain databases

Gene3D3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamPF00590. TP_methylase. 1 hit.
[Graphical view]
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUMT_SYNY3
AccessionPrimary (citable) accession number: Q55749
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways