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A1WWP8 (CYSG1_HALHL) 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:Hhal_1343
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira

Protein attributes

Sequence length484 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 – 484484Siroheme synthase 1 HAMAP-Rule MF_01646
PRO_0000330516

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 205205precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region220 – 484265Uroporphyrinogen-III C-methyltransferase By similarity
Region305 – 3073S-adenosyl-L-methionine binding By similarity
Region335 – 3362S-adenosyl-L-methionine binding By similarity

Sites

Active site2521Proton acceptor By similarity
Active site2741Proton donor By similarity
Binding site2291S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3101S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3871S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4161S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1301Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WWP8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: A45763C4C1213E0D

FASTA48452,541
        10         20         30         40         50         60 
MHHYPIFLKL HGCRCLVVGG GEAAARRAGD LLRAGARVEL IAPVLAAPCE QLLDTSPGEL 

        70         80         90        100        110        120 
HHRAEPFAAG MEEGAALVVG ASGDEATDRT VYEACRARGI PVNVAGRPSL STYITPVQVD 

       130        140        150        160        170        180 
RSPLQLAVSS GGAAPVLARQ IASRLETLLP AAYGRLARLA GRMREQVRVA LPDKDWRLRF 

       190        200        210        220        230        240 
WEQIFDGAAA ESVLAGREAE GEAELLRLLE QEQARPAPQG EVFLVGAGPG DPDLLTFRAL 

       250        260        270        280        290        300 
RLMQRADVVL YDRLAAPALL DLVRKEAERI PVGKRRGRHT LPQERINERL VELARAGKRV 

       310        320        330        340        350        360 
LRLKGGDPFL FGRGGEEIEG LIEQDIPFQV VPGISAAQGA ASYAGIPLTH RDYAQTCRLL 

       370        380        390        400        410        420 
TGHRRAGHPQ MKAHAPYRQD ETLIIYMGLV NLEAVCEQLC ECGLPPEHPA AVVAQATTPQ 

       430        440        450        460        470        480 
QRVVLGNLRT LAERVRAERV ESPALVVVGP TVQLHPRLGW YRGEAEDRDA AASIDPCWTG 


GMRD 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM62110.1.
RefSeqYP_001002912.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WWP8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349124.Hhal_1343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM62110; ABM62110; Hhal_1343.
GeneID4710901.
KEGGhha:Hhal_1343.
PATRIC22096985. VBIHalHal112047_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMANRVGQAY.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycHHAL349124:GI3I-1382-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_HALHL
AccessionPrimary (citable) accession number: A1WWP8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 6, 2007
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