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Q5FP95 (CYSG_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. 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:
Siroheme synthase

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase
    Short name=Urogen III methylase
    EC=2.1.1.107
    Alternative name(s):
    SUMT
    Uroporphyrinogen III methylase
    Short name=UROM
  2. Precorrin-2 dehydrogenase
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase
    EC=4.99.1.4
Gene names
Name:cysG
Ordered Locus Names:GOX2065
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme By similarity. HAMAP-Rule MF_01646

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP-Rule MF_01646

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP-Rule MF_01646

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP-Rule MF_01646

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP-Rule MF_01646

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

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

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.

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

Sequence similarities

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

In the C-terminal section; belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330514

Regions

Nucleotide binding37 – 382NAD By similarity
Nucleotide binding58 – 592NAD By similarity
Region1 – 222222precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region233 – 473241Uroporphyrinogen-III C-methyltransferase By similarity
Region318 – 3203S-adenosyl-L-methionine binding By similarity
Region348 – 3492S-adenosyl-L-methionine binding By similarity

Sites

Active site2651Proton acceptor By similarity
Active site2871Proton donor By similarity
Binding site2421S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3231S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site4011S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4301S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FP95 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: D03C0C346C837C48

FASTA47351,101
        10         20         30         40         50         60 
MNTQPHHSSP DSPQDGGWFP ISIRLSGARV LLVGGGEIAV NKGRLLLDHG ARIDVLAEKL 

        70         80         90        100        110        120 
HPAVQGWVEN GRVRHVGERA DEAVLRRLLP GCRLVYAATD SRDTNRQVAA LADELNIPVC 

       130        140        150        160        170        180 
AVDDPGPSSF ITPAQVRRGM VRVAVSTGGA APVLARRLRE QIETLLPEGT GRLATYMQSR 

       190        200        210        220        230        240 
RAFVSGRYPN VQDRKRIWED FLDGPGAEAA RSGDESRADA RLEVLLDGER KSGEVWLVGA 

       250        260        270        280        290        300 
GPGDPDLLTL KALHLMQNAD SVLYDNLVSP ALLDMVRRDA ELVFVGKQRD RHALPQDEIN 

       310        320        330        340        350        360 
REMVRRAQGG ERVLRLKGGD PFIFGRGGEE IEALVEAGVA FRLVPGISAA NGCAAYSGIP 

       370        380        390        400        410        420 
LTHRDCAQAC LFVTGHAKAD GVLDLPWDDM ADRRQTVVIY MGISTLPQLA AGLLGKGLPA 

       430        440        450        460        470 
DWPVAIVERG TQPRQRVFTG TLSTIAQQAA EAQVKSPALV IVGQVVRHRV VSP 

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References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW61801.1.
RefSeqYP_192457.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FP95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290633.GOX2065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW61801; AAW61801; GOX2065.
GeneID3248247.
KEGGgox:GOX2065.
PATRIC32612066. VBIGluOxy81109_2369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycGOXY290633:GHB3-2063-MONOMER.
UniPathwayUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01646. Siroheme_synth.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR016040. NAD(P)-bd_dom.
IPR012409. Sirohaem_synth.
IPR019478. Sirohaem_synthase_dimer_dom.
IPR006367. Sirohaem_synthase_N.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_GLUOX
AccessionPrimary (citable) accession number: Q5FP95
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 64 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