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Protein

Siroheme synthase 2

Gene

cysG2

Organism
Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))
Status
Reviewed-Annotation score: 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.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 sitei229 – 2291S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Active sitei252 – 2521Proton acceptorUniRule annotation
Active sitei274 – 2741Proton donorUniRule annotation
Binding sitei310 – 3101S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei387 – 3871S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei416 – 4161S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 232NADUniRule annotation
Nucleotide bindingi43 – 442NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciHHAL349124:GI3I-1982-MONOMER.
UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Names & Taxonomyi

Protein namesi
Recommended name:
Siroheme synthase 2UniRule annotation
Including the following 3 domains:
Uroporphyrinogen-III C-methyltransferase 2UniRule annotation (EC:2.1.1.107UniRule annotation)
Short name:
Urogen III methylase 2UniRule annotation
Alternative name(s):
SUMT 2UniRule annotation
Uroporphyrinogen III methylase 2UniRule annotation
Short name:
UROM 2UniRule annotation
Precorrin-2 dehydrogenase 2UniRule annotation (EC:1.3.1.76UniRule annotation)
Sirohydrochlorin ferrochelatase 2UniRule annotation (EC:4.99.1.4UniRule annotation)
Gene namesi
Name:cysG2UniRule annotation
Ordered Locus Names:Hhal_1933
OrganismiHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))
Taxonomic identifieri349124 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira
ProteomesiUP000000647 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Siroheme synthase 2PRO_0000330517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301PhosphoserineUniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi349124.Hhal_1933.

Structurei

3D structure databases

ProteinModelPortaliA1WYD5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 205205precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
BLAST
Regioni220 – 495276Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
BLAST
Regioni305 – 3073S-adenosyl-L-methionine bindingUniRule annotation
Regioni335 – 3362S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.UniRule annotation
In the C-terminal section; belongs to the precorrin methyltransferase family.UniRule annotation

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.
[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.

Sequencei

Sequence statusi: Complete.

A1WYD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHYPIFLNL HGRHCVVIGG NETAARKGED LLDSGAIITL IAPDLGGDCE
60 70 80 90 100
DLLQRYPDRA HHRAEDYKPG MEQGAALVLS ASGHDATDRL VYRQCTRLGI
110 120 130 140 150
PVNTVDRPEY CSYITPAVVD RSPLQVAITS GGAAPVLARQ VRSQIETLLP
160 170 180 190 200
TAYGRLAALA GRLRERVAAV LPTGRQRLRF WEQVFDGPAA ESMLAGRERE
210 220 230 240 250
AEQAMLELLR REQARRDERG EVYLVGAGPG DPDLLTFRAL RLMQRADVVL
260 270 280 290 300
YDHLAAPGLL RLVRKDAERI PVGKRRGQHT LPQEAINDKL IELAAAGKRV
310 320 330 340 350
LRLKGGDPFI FGRGGEEIEG LIEHGIPFQV VPAVTAAQGA AAYAGIPLTH
360 370 380 390 400
RDHAQSCRFL TGHRRHGALE LGQWAPFRSD ETLVVYMGLT HLETVSAQLQ
410 420 430 440 450
AGGLPPDQPA AAVDQATTPA QRVITAPLAE LPERVRTARL QGPALIVVGA
460 470 480 490
TVTLQPQLGW YHSSPNAEPA FPEHGCLRGE PRPTRHPAPA DTEQA
Length:495
Mass (Da):53,848
Last modified:February 6, 2007 - v1
Checksum:iD34306E7AF987ACA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000544 Genomic DNA. Translation: ABM62697.1.
RefSeqiWP_011814719.1. NC_008789.1.
YP_001003499.1. NC_008789.1.

Genome annotation databases

EnsemblBacteriaiABM62697; ABM62697; Hhal_1933.
KEGGihha:Hhal_1933.
PATRICi22098161. VBIHalHal112047_1908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000544 Genomic DNA. Translation: ABM62697.1.
RefSeqiWP_011814719.1. NC_008789.1.
YP_001003499.1. NC_008789.1.

3D structure databases

ProteinModelPortaliA1WYD5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349124.Hhal_1933.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM62697; ABM62697; Hhal_1933.
KEGGihha:Hhal_1933.
PATRICi22098161. VBIHalHal112047_1908.

Phylogenomic databases

eggNOGiCOG0007.
HOGENOMiHOG000290518.
KOiK02302.
OMAiLHQQLAW.
OrthoDBiEOG6DRPFR.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.
BioCyciHHAL349124:GI3I-1982-MONOMER.

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.
[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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 244 / SL1.

Entry informationi

Entry nameiCYSG2_HALHL
AccessioniPrimary (citable) accession number: A1WYD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 6, 2007
Last modified: May 27, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.