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A0KLD7 (CYSG1_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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 1

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase 1
    Short name=Urogen III methylase 1
    EC=2.1.1.107
    Alternative name(s):
    SUMT 1
    Uroporphyrinogen III methylase 1
    Short name=UROM 1
  2. Precorrin-2 dehydrogenase 1
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase 1
    EC=4.99.1.4
Gene names
Name:cysG1
Ordered Locus Names:AHA_2578
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length463 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 – 463463Siroheme synthase 1 HAMAP-Rule MF_01646
PRO_0000330486

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region215 – 463249Uroporphyrinogen-III C-methyltransferase By similarity
Region300 – 3023S-adenosyl-L-methionine binding By similarity
Region330 – 3312S-adenosyl-L-methionine binding By similarity

Sites

Active site2471Proton acceptor By similarity
Active site2691Proton donor By similarity
Binding site2241S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3051S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3821S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KLD7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 8BB6D209F187B3DB

FASTA46350,392
        10         20         30         40         50         60 
MDFLPLFCQL QHKPVLIVGG GEVAVRKARL LLDAKARVTI NAPHLEPQLM SWAEQGLLTV 

        70         80         90        100        110        120 
CAADFHPELL DGKWLVIAAT NQPEVNQQVF NEANRRQIFC NVVDSPAHCS AIMPAIIDRS 

       130        140        150        160        170        180 
PLMVAISSAG SAPLLSRQLR EKIEALLPQH LGQLATLAGK LRERVKAIPD KLARRRFWER 

       190        200        210        220        230        240 
LFSHERLACQ LARGQQQAAE ESVAELLNEP QQSKGSVTLV GAGPGDAGLL TLNGLQQLQQ 

       250        260        270        280        290        300 
ADVVVYDRLV SQEVLAHVRR DAERIFVGKE AGCHCVPQQA INQLLLEQAR LGKQVVRLKG 

       310        320        330        340        350        360 
GDPFIFGRGG EELETLAEAG IPFSVVPGIT AASGCAAYSG IPLTHRDHAQ RVQFITGHDK 

       370        380        390        400        410        420 
EGNIAQEWPA LATPRQTLVF YMGLAHAGRI QDELQTHGLP GHTPVALVEQ GTRLQQRVVR 

       430        440        450        460 
GKLQQLAQLA TQVESPSLII IGSVVTLADK LDWYGEANTL AGV 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000462 Genomic DNA. Translation: ABK39337.1.
RefSeqYP_857088.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KLD7.
SMRA0KLD7. Positions 1-454.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380703.AHA_2578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK39337; ABK39337; AHA_2578.
GeneID4490900.
KEGGaha:AHA_2578.
PATRIC20782750. VBIAerHyd135212_2577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMADAWYAIA.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycAHYD380703:GH2M-2578-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.
PROSITEPS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG1_AERHH
AccessionPrimary (citable) accession number: A0KLD7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 12, 2006
Last modified: June 11, 2014
This is version 58 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