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Reviewed, UniProtKB/Swiss-Prot Q21K21 (CYSG_SACD2)

Last modified February 9, 2010. Version 33. 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: Sde_1698
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
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. HAMAP MF_01646

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 – 458458Siroheme synthase HAMAP MF_01646
PRO_0000330551

Regions

Region218 – 458241Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q21K21-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 00C40A4EBBA40706

FASTA45850,119
        10         20         30         40         50         60 
MDYLPLFFDL KAKPCLIVGG GTIATRKARL LHKAGAKLHV VAPKVSEELE KLVAASNGKV 

        70         80         90        100        110        120 
FKQEYDQTFL DDVILVISAT DIDAVNSVVA ADCHAIKLPV NVVDSPALCS VIMPAIIDRS 

       130        140        150        160        170        180 
PLIIGVTSGG EAPVLARRVR SMLESSIPAA YGQLAQLASK FRQRAKDVFE NGDLRRRFWE 

       190        200        210        220        230        240 
NILNGPIAEK VLGGNLAAAE QLIEAQLDSA SVEKTGEVYL VGAGPGDPDL LTFKALRLMQ 

       250        260        270        280        290        300 
QAEVVLYDRL VSEPILEMTR RDAERIYVGK KRAEHAVPQQ KINQMLLELA QQGKRVLRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEEIDLLAEH KIPFQVVPGI TAASGCASYS GIPLTHRDYS QSVRFITGHL 

       370        380        390        400        410        420 
QEGKENFRWS EFVDKQQTLV FYMGLAGLET ICSKLIEYGK SPSTPAALIE RGTLPEQRVH 

       430        440        450 
VSDLAGLAAK IEGLDVHAPT LLIIGDVVRC HEKLNWYK 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed: 18516288] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80958.1.
RefSeqYP_527170.1.

3D structure databases

SMRQ21K21. Positions 1-458.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ21K21.

Genome annotation databases

GeneID3966485.
GenomeReviewsGene locus Sde_1698 in contig CP000282_GR.
KEGGsde:Sde_1698.
NMPDRfig|203122.1.peg.4259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHBG730212.
OMAMCRRDAE.
PhylomeDBQ21K21.

Enzyme and pathway databases

BioCycSDEG203122:SDE_1698-MONOMER.

Family and domain databases

HAMAPMF_01646. Siroheme_synth.
[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_SACD2
AccessionPrimary (citable) accession number: Q21K21
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 18, 2006
Last modified: February 9, 2010
This is version 33 of the entry and version 1 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