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Q1QAX7 (CYSG_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. 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:Pcryo_1397
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length523 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 caution

The sequence ABE75176.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330547

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region231 – 523293Uroporphyrinogen-III C-methyltransferase By similarity
Region316 – 3183S-adenosyl-L-methionine binding By similarity
Region346 – 3472S-adenosyl-L-methionine binding By similarity

Sites

Active site2631Proton acceptor By similarity
Active site2851Proton donor By similarity
Binding site2401S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3211S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3981S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4271S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QAX7 [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."
US DOE Joint Genome Institute
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].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE75176.1. Different initiation.
RefSeqYP_580660.1. NC_007969.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_1397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE75176; ABE75176; Pcryo_1397.
GeneID4033707.
KEGGpcr:Pcryo_1397.
PATRIC23062331. VBIPsyCry128170_1490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-1427-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 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 11, 2014
This is version 60 of the entry and version 2 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