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Protein

Precorrin-2 dehydrogenase

Gene

sirC

Organism
Bacillus megaterium
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis. It is unable to oxidize precorrin-3.2 Publications

Catalytic activityi

Precorrin-2 + NAD+ = sirohydrochlorin + NADH.2 Publications

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.
Proteins known to be involved in this subpathway in this organism are:
  1. Precorrin-2 dehydrogenase (sirC)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathwayi: siroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.
Proteins known to be involved in this subpathway in this organism are:
  1. Precorrin-2 dehydrogenase (sirC), Precorrin-2 dehydrogenase (AWX17_14375)
This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 212NADBy similarity
Nucleotide bindingi41 – 422NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.3.1.76. 656.
UniPathwayiUPA00148; UER00222.
UPA00262; UER00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Precorrin-2 dehydrogenase (EC:1.3.1.76)
Gene namesi
Name:sirC
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 981N → A: 4-fold decrease in the dehydrogenase activity. 1 Publication
Mutagenesisi101 – 1011S → A: 1.4-fold increase in the dehydrogenase activity. 1 Publication
Mutagenesisi101 – 1011S → D: 2.8-fold increase in the dehydrogenase activity. 1 Publication
Mutagenesisi102 – 1021S → A: 2.3-fold increase in the dehydrogenase activity. 1 Publication
Mutagenesisi105 – 1051D → A: 3.2-fold increase in the dehydrogenase activity. 1 Publication
Mutagenesisi124 – 1241S → A: 3-fold decrease in the dehydrogenase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Precorrin-2 dehydrogenasePRO_0000097773Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi545693.BMQ_4926.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi13 – 164Combined sources
Helixi20 – 2910Combined sources
Helixi30 – 323Combined sources
Beta strandi36 – 394Combined sources
Helixi45 – 528Combined sources
Beta strandi57 – 593Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 703Combined sources
Beta strandi72 – 765Combined sources
Helixi82 – 909Combined sources
Beta strandi96 – 983Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi119 – 1246Combined sources
Helixi130 – 14314Combined sources
Helixi147 – 16418Combined sources
Helixi169 – 17810Combined sources
Helixi182 – 1865Combined sources
Helixi188 – 19912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DFZX-ray2.30A/B1-202[»]
ProteinModelPortaliP61818.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61818.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108Z73. Bacteria.
COG1648. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR028281. Sirohaem_synthase_central.
IPR006367. Sirohaem_synthase_N.
[Graphical view]
PfamiPF13241. NAD_binding_7. 1 hit.
PF14824. Sirohm_synth_M. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01470. cysG_Nterm. 1 hit.

Sequencei

Sequence statusi: Complete.

P61818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTVMLDLKG RSVLVVGGGT IATRRIKGFL QEGAAITVVA PTVSAEINEW
60 70 80 90 100
EAKGQLRVKR KKVGEEDLLN VFFIVVATND QAVNKFVKQH IKNDQLVNMA
110 120 130 140 150
SSFSDGNIQI PAQFSRGRLS LAISTDGASP LLTKRIKEDL SSNYDESYTQ
160 170 180 190 200
YTQFLYECRV LIHRLNVSKS RKHELLTEII DDQYRLSLVK QREFLQQIEK

YK
Length:202
Mass (Da):22,970
Last modified:June 7, 2004 - v1
Checksum:i7AA89B591622DEAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ509159 Genomic DNA. Translation: CAD48923.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ509159 Genomic DNA. Translation: CAD48923.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DFZX-ray2.30A/B1-202[»]
ProteinModelPortaliP61818.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi545693.BMQ_4926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108Z73. Bacteria.
COG1648. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00222.
UPA00262; UER00222.
BRENDAi1.3.1.76. 656.

Miscellaneous databases

EvolutionaryTraceiP61818.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR028281. Sirohaem_synthase_central.
IPR006367. Sirohaem_synthase_N.
[Graphical view]
PfamiPF13241. NAD_binding_7. 1 hit.
PF14824. Sirohm_synth_M. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01470. cysG_Nterm. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSIRC_BACME
AccessioniPrimary (citable) accession number: P61818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: December 9, 2015
This is version 59 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.