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A9H259 (CYSG_GLUDA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:GDI0165, Gdia_2235
OrganismGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]
Taxonomic identifier272568 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length470 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 – 470470Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330513

Regions

Nucleotide binding28 – 292NAD By similarity
Nucleotide binding49 – 502NAD By similarity
Region1 – 213213precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region224 – 470247Uroporphyrinogen-III C-methyltransferase By similarity
Region309 – 3113S-adenosyl-L-methionine binding By similarity
Region339 – 3402S-adenosyl-L-methionine binding By similarity

Sites

Active site2561Proton acceptor By similarity
Active site2781Proton donor By similarity
Binding site2331S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3141S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3921S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4211S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9H259 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 70D8FF743EA97B96

FASTA47050,124
        10         20         30         40         50         60 
MSDATDPGWF PLALRLRGAR VVVVGGGGIA LNKVRLLLAH AARIDILAPR LEDTLAAWQA 

        70         80         90        100        110        120 
EGRITHIAGE ATPDRVRALL PGSRLVYAAT DDRAVNRAVA AQADALNIPV CAVDDPEPSS 

       130        140        150        160        170        180 
FITPAQIHRG PVRIAISTGG AAPVLARRLR ERIEAVMPAG LDALARFLQA ERAHVVAACP 

       190        200        210        220        230        240 
DIGRRRRVWE DFLDGPGGEA AQRGEHAAAR QVLDHLLAGA QTGGEVWLVG AGPGDPDLLT 

       250        260        270        280        290        300 
LRALHLMQNA DSVLYDQLLP PALMDRVRRD AERVFVGKQR DRHTMPQDDI NAELIRRARA 

       310        320        330        340        350        360 
GERVLRLKGG DPFIFGRGGE EIEALMAAGI PFQVVPGITA ASGCAAYAGI PLTHRDCAQS 

       370        380        390        400        410        420 
CLFVTGHARR DGTLDLPWDS MARPGQTIAI YMGVTALPDL CTMLVRHGLP PDWPAAVVER 

       430        440        450        460        470 
GTRPDQRVLT GTLADLPALA RAHAVGSPAL VLVGQVVRHR VVTPPPLSGT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM889285 Genomic DNA. Translation: CAP54108.1.
CP001189 Genomic DNA. Translation: ACI51990.1.
RefSeqYP_001600455.1. NC_010125.1.
YP_002276605.1. NC_011365.1.

3D structure databases

ProteinModelPortalA9H259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272568.GDI_0165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI51990; ACI51990; Gdia_2235.
CAP54108; CAP54108; GDI0165.
GeneID5788693.
6975664.
KEGGgdi:GDI_0165.
gdj:Gdia_2235.
PATRIC22052918. VBIGluDia203729_2239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMALHQQLAW.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycGDIA272568:GJPS-171-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_GLUDA
AccessionPrimary (citable) accession number: A9H259
Secondary accession number(s): B5ZEK0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 54 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