Reviewed, UniProtKB/Swiss-Prot A0KP37 (CYSG2_AERHH)

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:	AHA_3568

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
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.

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 – 470	470	Siroheme synthase 2 HAMAP MF_01646		PRO_0000330487
Regions
	Region	216 – 456	241	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	A0KP37-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 9E572A53CAAF5A6A	FASTA	470	50,861
	10 20 30 40 50 60 MDYLPMFAKL DGRPVLLVGG GEVALRKARL LLAAGARLTL VSPELEPDFH QFADRFTHLA 70 80 90 100 110 120 ERFTPAHLTG QILVVAATDD LEVNALVYQS ANQLGLFVNV VDDPKRSSFI FPSIIDRSPI 130 140 150 160 170 180 MVAVSSGGKA PVLVRLLRER LESLLPRHLG ALAELSGRVR DQAKRVLSSI SDRRRFWERA 190 200 210 220 230 240 FASNTLAGLI EKEDWQGAEQ WLNDGLDQAK NEVGEVVLVG AGPGDPGLLT LKALQQIQQA 250 260 270 280 290 300 EVVLYDQLVS PEILDLVRRD ATLVSVGKKA GAHSVPQEET NRLLVEYAKA GNRVVRLKGG 310 320 330 340 350 360 DPFMFGRGGE ELEVLAEEGI PFSVVPGITA AAGATAYAGI PLTHRDHAQS AVFITGHCQI 370 380 390 400 410 420 DGKEPDWQQL AATSQTLVIY MGLMRSEHIQ QQLVSHGRSS ATPIAIIERG TTARQRVLTG 430 440 450 460 470 TLADLAELAA QAVSPSLIVI GEVVALRERL AWFGEGQQQG TCDLKLVSLA

References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000462 Genomic DNA. Translation: ABK38644.1.
RefSeq	YP_858038.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4488263.
GenomeReviews	Gene locus AHA_3568 in contig CP000462_GR.
KEGG	aha:AHA_3568.
TIGR	AHA_3568.
Phylogenomic databases
OMA	A0KP37. DKLVPQQ.
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR000878. 4pyrrol_Mease. IPR006366. CobA_cysG_C. IPR019478. Sirohaem_synthase_dimer_dom. IPR006367. Sirohaem_synthase_N. IPR003043. Uropor_MeTrfase_CS. [Graphical view]
Pfam	PF10414. CysG_dimeriser. 1 hit. 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_AERHH

Accession

Primary (citable) accession number: A0KP37

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	December 12, 2006
Last modified:	June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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