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B4SHI1 (CYOE_STRM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Protoheme IX farnesyltransferase

EC=2.5.1.-
Alternative name(s):
Heme B farnesyltransferase
Heme O synthase
Gene names
Name:cyoE
Ordered Locus Names:Smal_0319
OrganismStenotrophomonas maltophilia (strain R551-3) [Complete proteome] [HAMAP]
Taxonomic identifier391008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group By similarity. HAMAP-Rule MF_00154

Pathway

Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1. HAMAP-Rule MF_00154

Subcellular location

Cell inner membrane; Multi-pass membrane protein Potential HAMAP-Rule MF_00154.

Miscellaneous

Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature By similarity.

Sequence similarities

Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.

Ontologies

Keywords
   Biological processHeme biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processheme O biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotoheme IX farnesyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Protoheme IX farnesyltransferase HAMAP-Rule MF_00154
PRO_1000096927

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane45 – 6521Helical; Potential
Transmembrane93 – 11321Helical; Potential
Transmembrane114 – 13421Helical; Potential
Transmembrane141 – 16121Helical; Potential
Transmembrane172 – 19221Helical; Potential
Transmembrane223 – 24321Helical; Potential
Transmembrane244 – 26421Helical; Potential
Transmembrane277 – 29721Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
B4SHI1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 00C3B34D22A1F334

FASTA29733,163
        10         20         30         40         50         60 
MFSNYRQYWD LTKPKVVALI VFTALVGMVL AIPGVPSWEQ VRAGVLGFLG IWLAASAAAA 

        70         80         90        100        110        120 
INQLLDAHID AQMARTSWRP LVVGKVKPWQ VLVFASVLIV LSMVILVLWV NLITAVLTFA 

       130        140        150        160        170        180 
SLIGYAVIYT VYLKRATSQN IVIGGLAGAM PPMLGWAAVT GMQGSSDWAY SSLLVLIIFI 

       190        200        210        220        230        240 
WTPPHFWALA IFRREDYAKA EIPMLPVTHG VVHTRKQIMV YSVVLALVCL LPYLVGMSGA 

       250        260        270        280        290 
FYLGGAIVLN AVFLWYAWRM LDPPDELFSM KMFYYSIVYL MALFAFLLVD HWILPWL 

« Hide

References

[1]"Complete sequence of Stenotrophomonas maltophilia R551-3."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Taghavi S., Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R551-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001111 Genomic DNA. Translation: ACF50024.1.
RefSeqYP_002026707.1. NC_011071.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391008.Smal_0319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF50024; ACF50024; Smal_0319.
GeneID6478115.
KEGGsmt:Smal_0319.
PATRIC23705456. VBISteMal40512_0320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0109.
HOGENOMHOG000237291.
KOK02301.
OMAYYEMTKP.
OrthoDBEOG6DVJQB.
ProtClustDBPRK04375.

Enzyme and pathway databases

BioCycSMAL391008:GH1H-331-MONOMER.
UniPathwayUPA00834; UER00712.

Family and domain databases

HAMAPMF_00154. CyoE_CtaB.
InterProIPR006369. Protohaem_IX_farnesylTrfase.
IPR000537. UbiA_prenyltransferase.
[Graphical view]
PfamPF01040. UbiA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01473. cyoE_ctaB. 1 hit.
PROSITEPS00943. UBIA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYOE_STRM5
AccessionPrimary (citable) accession number: B4SHI1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 41 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