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Q6F8G6 (CYSG_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ACIAD2934
OrganismAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length457 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 – 457457Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330484

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region216 – 457242Uroporphyrinogen-III C-methyltransferase By similarity
Region301 – 3033S-adenosyl-L-methionine binding By similarity
Region331 – 3322S-adenosyl-L-methionine binding By similarity

Sites

Active site2481Proton acceptor By similarity
Active site2701Proton donor By similarity
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3061S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3831S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4121S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1291Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F8G6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: F3076FEFEA6830A2

FASTA45750,431
        10         20         30         40         50         60 
MEIFPISLKL QQQRCLIVGG GHIAYRKAIL LVKAGAILDI VAPDIDPQLM SLIEQSAGTA 

        70         80         90        100        110        120 
YVKLFEDHDL DRVYRLVIAA TDNADVNKRV FEQAELRNLL VNSVDDIPNC RFMVPAIIDR 

       130        140        150        160        170        180 
SPLLISVASN GASPVLSRQL RTQIETLVPH GMGKLAEFSG QWRSRVKAQI TNPDERRIFW 

       190        200        210        220        230        240 
EELYASPLKE QVFNDNLDIA NQMMTQSLAE WTAPKGEVYL VGAGPGDPEL LTLKALRLMQ 

       250        260        270        280        290        300 
QADVVIYDRL VSAPILELCR RDAEKVYVGK ARSNHSVPQE GINALLVKYA QAGKRVCRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEEIQELFAA GIPFQVVPGI TAASGCSAYA GIPLTHRDYA QSVRFLTGHL 

       370        380        390        400        410        420 
KEGSPELPWS ELVYENQTLV LYMGLVGLEH ICQQLIAHGQ RPDMPVALVS KGTTPEQKVV 

       430        440        450 
VGTLSNIASK IAEYQIHAPT LTIIGEVVSL REQLQWL 

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References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33305 / BD413 / ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG69649.1.
RefSeqYP_047471.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6F8G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62977.ACIAD2934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG69649; CAG69649; ACIAD2934.
GeneID2878421.
KEGGaci:ACIAD2934.
PATRIC20743379. VBIAciSp98416_2619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycASP62977:GJVV-2720-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_ACIAD
AccessionPrimary (citable) accession number: Q6F8G6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 19, 2004
Last modified: June 11, 2014
This is version 74 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