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Q4FSU1

- CYSG_PSYA2

UniProt

Q4FSU1 - CYSG_PSYA2

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Protein

Siroheme synthase

Gene
cysG, Psyc_1065
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.UniRule annotation
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.UniRule annotation
Precorrin-2 + NAD+ = sirohydrochlorin + NADH.UniRule annotation
Siroheme + 2 H+ = sirohydrochlorin + Fe2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei256 – 2561S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Active sitei279 – 2791Proton acceptor By similarity
Active sitei301 – 3011Proton donor By similarity
Binding sitei337 – 3371S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei414 – 4141S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei443 – 4431S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 232NAD By similarity
Nucleotide bindingi43 – 442NAD By similarity

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. precorrin-2 dehydrogenase activity Source: UniProtKB-HAMAP
  3. sirohydrochlorin ferrochelatase activity Source: UniProtKB-EC
  4. uroporphyrin-III C-methyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-HAMAP
  2. siroheme biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NAD, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciPARC259536:GI3A-1096-MONOMER.
UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Names & Taxonomyi

Protein namesi
Recommended name:
Siroheme synthase
Including the following 3 domains:
Uroporphyrinogen-III C-methyltransferase (EC:2.1.1.107)
Short name:
Urogen III methylase
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name:
UROM
Precorrin-2 dehydrogenase (EC:1.3.1.76)
Sirohydrochlorin ferrochelatase (EC:4.99.1.4)
Gene namesi
Name:cysG
Ordered Locus Names:Psyc_1065
OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
Taxonomic identifieri259536 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000000546: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Siroheme synthaseUniRule annotationPRO_0000330546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi259536.Psyc_1065.

Structurei

3D structure databases

ProteinModelPortaliQ4FSU1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarityAdd
BLAST
Regioni247 – 549303Uroporphyrinogen-III C-methyltransferase By similarityAdd
BLAST
Regioni332 – 3343S-adenosyl-L-methionine binding By similarity
Regioni362 – 3632S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

In the C-terminal section; belongs to the precorrin methyltransferase family.

Phylogenomic databases

eggNOGiCOG0007.
HOGENOMiHOG000290518.
KOiK02302.
OMAiLHQQLAW.
OrthoDBiEOG6DRPFR.

Family and domain databases

Gene3Di1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01646. Siroheme_synth.
InterProiIPR000878. 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]
PfamiPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEiPS00840. SUMT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4FSU1-1 [UniParc]FASTAAdd to Basket

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MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGACITV LAPSINHEIQ    50
ALLSSSKHEL IYEHYNKTYM TNSRVIIAAT DDERLNHQIH ADATALNIPV 100
NVVDTPHLCD FIFPAIVDRN PIVIGISSNG KAPVLARLLR ARLETLIPQG 150
YGKLAKLAGE FRGDVKAKIP TLTGRRQFWE RAFEGKVSQL MFAGNENEAL 200
AQLQADLDNT AASITAKDAT DDNGLSTAST SAPAIANEFT AARNTMGEVY 250
IVGAGPGDPE LLTFKALRLM QQADIVYYDA LVSPQVLDLC RRDADKVFVG 300
KKRRNHAVAQ LGINELLVNS AKEGRRVVRL KGGDPFIFGR GGEEIESLRA 350
HNIPYQVVPG ITAANAAASY AGIPLTHRDH SQSVRFVTGF LKAGAPNNNF 400
KNFLDTDETV VFYMGLHSLP RLTEGLIDAG RSAETPIAIV SNASMPNQQV 450
LTGTLASIVE LQEKNQLPTP ALLIMGDVVS LHHDLAWYNL HNQQHNQNTS 500
ETDNNWLRGG TATTPKSNAQ FNAHQQAHAL SMITNLATED GDLEQLIIG 549
Length:549
Mass (Da):59,727
Last modified:April 29, 2008 - v2
Checksum:i019AACCDA20937C4
GO

Sequence cautioni

The sequence AAZ18917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000082 Genomic DNA. Translation: AAZ18917.1. Different initiation.
RefSeqiYP_264351.1. NC_007204.1.

Genome annotation databases

EnsemblBacteriaiAAZ18917; AAZ18917; Psyc_1065.
GeneIDi3514951.
KEGGipar:Psyc_1065.
PATRICi23056681. VBIPsyArc98534_1258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000082 Genomic DNA. Translation: AAZ18917.1 . Different initiation.
RefSeqi YP_264351.1. NC_007204.1.

3D structure databases

ProteinModelPortali Q4FSU1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 259536.Psyc_1065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ18917 ; AAZ18917 ; Psyc_1065 .
GeneIDi 3514951.
KEGGi par:Psyc_1065.
PATRICi 23056681. VBIPsyArc98534_1258.

Phylogenomic databases

eggNOGi COG0007.
HOGENOMi HOG000290518.
KOi K02302.
OMAi LHQQLAW.
OrthoDBi EOG6DRPFR.

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00211 .
UPA00148 ; UER00222 .
UPA00262 ; UER00211 .
UPA00262 ; UER00222 .
UPA00262 ; UER00376 .
BioCyci PARC259536:GI3A-1096-MONOMER.

Family and domain databases

Gene3Di 1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPi MF_01646. Siroheme_synth.
InterProi IPR000878. 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 ]
Pfami PF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMi SSF53790. SSF53790. 1 hit.
TIGRFAMsi TIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEi PS00840. SUMT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
    Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
    Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17307 / 273-4.

Entry informationi

Entry nameiCYSG_PSYA2
AccessioniPrimary (citable) accession number: Q4FSU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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