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Reviewed, UniProtKB/Swiss-Prot Q1QAX7 (CYSG_PSYCK)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Siroheme synthase
Including the following 3 domains:
    1- Recommended name:
            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- Recommended name:
            Precorrin-2 dehydrogenase
              EC=1.3.1.76
    3- Recommended name:
            Sirohydrochlorin ferrochelatase
              EC=4.99.1.4
Gene names
Name: cysG
Ordered Locus Names: Pcryo_1397
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme By similarity.

Catalytic activity

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

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

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

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

Pathway

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

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

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

Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646

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

Sequence similarities

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Siroheme synthase HAMAP MF_01646
PRO_0000330547

Regions

Region233 – 475243Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q1QAX7-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 8D65D4497A36F4B7

FASTA52356,795
        10         20         30         40         50         60 
MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGACITV LAPSISHEIQ ALLSDSKHAL 

        70         80         90        100        110        120 
IYENYNKTYM TDSRVIIAAT DDETLNHQIH SDATALNIPV NVVDTPHLCD FIFPAIVDRN 

       130        140        150        160        170        180 
PIVIGISSNG KAPVLARLLR ARLETLIPQG YGKLAKLAGE FRGDVKAKIP TLTGRRQFWE 

       190        200        210        220        230        240 
QVFEGKVSQL MFSGNENEAI AQLQADLDNT AANITAKNAT DESTEAQNTM GEVYIVGAGP 

       250        260        270        280        290        300 
GDPELLTFKA LRLMQQADIV YYDALVSPQV LDLCRRDADK VFVGKKRSNH AVAQLGINEL 

       310        320        330        340        350        360 
LVNSAKEGRR VVRLKGGDPF IFGRGGEEIE SLRSHNVPYQ VVPGITAANA AASYAGIPLT 

       370        380        390        400        410        420 
HRDHSQSVRF VTGFLKAGAP NNNFKSFLNT DETVVFYMGL HSLPRLTQGL IDAGRSAKTP 

       430        440        450        460        470        480 
IAIVSNASMP NQQVLTGTLA SIVELQAQHQ LPTPALLIMG DVVSLHHDLA WYNNKKTSEN 

       490        500        510        520 
DNNWLRGGTA TTPKPNPNQQ AHALSMIANL ATEDGGLEQL VID 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000323 Genomic DNA. Translation: ABE75176.1. Different initiation.
RefSeqYP_580660.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4033707.
GenomeReviewsGene locus Pcryo_1397 in contig CP000323_GR.
KEGGpcr:Pcryo_1397.
NMPDRfig|335284.3.peg.1549.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1QAX7.

Enzyme and pathway databases

BioCycPCRY335284:PCRYO_1397-MON.

Family and domain databases

HAMAPMF_01646.
[Tree]
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA_cysG_C.
IPR016040. NAD(P)-bd_dom.
IPR019478. Sirohaem_synthase_dimer_dom.
IPR006367. Sirohaem_synthase_N.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1010.10. 4pyrrole_Mease_sub1. 1 hit.
G3DSA:3.30.950.10. 4pyrrole_Mease_sub2. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF10414. CysG_dimeriser. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. False negative.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_PSYCK
AccessionPrimary (citable) accession number: Q1QAX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: June 16, 2009
This is version 25 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents