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O34744 (SUMT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 82. 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:sumT
Synonyms:ylnD
Ordered Locus Names:BSU15610
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Induction

Up-regulated by sulfur starvation and repressed by cysteine. Also induced by O-acetyl-L-serine (OAS), a direct precursor of cysteine, maybe via inactivation of a putative transcriptional repressor of the cysH operon whose activity is controlled by the intracellular levels of OAS. Ref.3

Sequence similarities

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Uroporphyrinogen-III C-methyltransferase
PRO_0000378491

Regions

Region87 – 893S-adenosyl-L-methionine binding By similarity

Sites

Binding site111S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1171S-adenosyl-L-methionine By similarity
Binding site1701S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O34744 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B1D28A495D27DA85

FASTA25728,516
        10         20         30         40         50         60 
MGKVYIVGAG PGDPDLLTIK ALKAIEKADV ILYDRLVNKE ILQYAKEQAD LIYCGKLPDF 

        70         80         90        100        110        120 
HTMKQETINR FLVKYAQKGK MVVRLKGGDP FVFGRGGEEA ECLSENGIPF EIIPGITSGI 

       130        140        150        160        170        180 
AAAAYAGIPV THRDAGSNVA FVTGHYKKEE DFEEKWKALA TGIDTLVIYM GIKNVQQIER 

       190        200        210        220        230        240 
KLLENGRDGS TPAAFIHWGT TDKQKSVFCT VDTLSETVIK ENITNPSLIV IGNVVNYHYK 

       250 
LEWFESELKK QDLSEAL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of the pyr operon."
Foulger D., Errington J.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis."
Mansilla M.C., Albanesi D., de Mendoza D.
J. Bacteriol. 182:5885-5892(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: 168 / JH642.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000974 Genomic DNA. Translation: CAA04413.1.
AL009126 Genomic DNA. Translation: CAB13435.1.
PIRD69877.
RefSeqNP_389444.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34744.
SMRO34744. Positions 2-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU15610.

Proteomic databases

PaxDbO34744.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13435; CAB13435; BSU15610.
GeneID936712.
KEGGbsu:BSU15610.
PATRIC18974929. VBIBacSub10457_1656.

Organism-specific databases

GenoListBSU15610. [Micado]

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290519.
KOK02303.
OMAKWENLAK.
OrthoDBEOG6BGNXZ.
ProtClustDBCLSK887284.

Enzyme and pathway databases

BioCycBSUB:BSU15610-MONOMER.
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_BACSU
AccessionPrimary (citable) accession number: O34744
Secondary accession number(s): Q796I5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList