Reviewed, UniProtKB/Swiss-Prot A4SRH0 (CYSG2_AERS4)

Names and origin

Protein names

Recommended name:
    Siroheme synthase 2
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:	cysG2
Ordered Locus Names:	ASA_3524

Organism

Aeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]

Taxonomic identifier

382245 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Multifunctional enzyme that catalyze 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 consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme By similarity.
Catalytic activity	S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
Sequence similarities	Belongs to the precorrin methyltransferase family.
Sequence caution	The sequence ABO91492.1 differs from that shown. Reason: Frameshift at position 22.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis Porphyrin biosynthesis
Ligand	NAD S-adenosyl-L-methionine
Molecular function	Lyase Methyltransferase Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cobalamin biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW siroheme biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	binding Inferred from electronic annotation. Source: InterPro precorrin-2 dehydrogenase activity Inferred from electronic annotation. Source: HAMAP sirohydrochlorin ferrochelatase activity Inferred from electronic annotation. Source: EC uroporphyrin-III C-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 480	480	Siroheme synthase 2		PRO_0000330490
Regions
	Region	216 – 456	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A4SRH0-1 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 73EA4371971ABAA8	FASTA	480	51,976
	10 20 30 40 50 60 MDYLPMFARL EGRPVLLVGG GEVALRKARL LLAAGARLTL VSPEIEPEFA EFAGRFTHLV 70 80 90 100 110 120 ERFTPAHLAG QLLVVAATDN LEVNALVYQS ANQLGLFVNV VDDPKRSSFI FPSIIDRSPL 130 140 150 160 170 180 MVAVSSGGKA PVLVRLLRER LESLLPRHLG GLTELSGRVR DKAKQVLSSI SDRRRFWERA 190 200 210 220 230 240 FASNTLAGLI EKQDWQSAET WLNDGLDKAQ SEVGEVVLVG AGPGDPGLLT LKALQQIQQA 250 260 270 280 290 300 EVVLYDQLVS PEILDLVRRD ATLVSVGKKA GAHSVPQEET NRLLVEYARA GNRVVRLKGG 310 320 330 340 350 360 DPFMFGCGGE ELEVLAAEGI PFSVVPGITA AAGATAYAGI PLTHRDHAQS AVFITGHCQK 370 380 390 400 410 420 EGKEPDWQQL AVTQQTLVIY MGLMRSEHIQ QQLVSHGRSC TTPIAIIEWG TTARQRVLTG 430 440 450 460 470 480 TLAELAVLAQ QAVSPSLIVI GEVVSLRKQL AWFGEKSGEK RDVQAGTDMN GCDLKLVNLA

References

[1]

"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449." Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000644 Genomic DNA. Translation: ABO91492.1. Frameshift.
RefSeq	YP_001143240.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4995755.
GenomeReviews	Gene locus ASA_3524 in contig CP000644_GR.
KEGG	asa:ASA_3524.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR000878. 4pyrrol_Mease. IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR006367. CysG_synth_N. IPR016040. NAD(P)-bd. IPR003043. Uropor_MeTrfase_CS. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF00590. TP_methylase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01469. cobA_cysG_Cterm. 1 hit. TIGR01470. cysG_Nterm. 1 hit.
PROSITE	PS00839. SUMT_1. 1 hit. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG2_AERS4

Accession

Primary (citable) accession number: A4SRH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	November 25, 2008
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)