Reviewed, UniProtKB/Swiss-Prot A1WYD5 (CYSG2_HALHL)

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:	Hhal_1933

Organism

Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]

Taxonomic identifier

349124 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Halorhodospira

Protein attributes

Sequence length	495 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 – 495	495	Siroheme synthase 2 HAMAP MF_01646		PRO_0000330517
Regions
	Region	222 – 464	243	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	A1WYD5-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: D34306E7AF987ACA	FASTA	495	53,848
	10 20 30 40 50 60 MDHYPIFLNL HGRHCVVIGG NETAARKGED LLDSGAIITL IAPDLGGDCE DLLQRYPDRA 70 80 90 100 110 120 HHRAEDYKPG MEQGAALVLS ASGHDATDRL VYRQCTRLGI PVNTVDRPEY CSYITPAVVD 130 140 150 160 170 180 RSPLQVAITS GGAAPVLARQ VRSQIETLLP TAYGRLAALA GRLRERVAAV LPTGRQRLRF 190 200 210 220 230 240 WEQVFDGPAA ESMLAGRERE AEQAMLELLR REQARRDERG EVYLVGAGPG DPDLLTFRAL 250 260 270 280 290 300 RLMQRADVVL YDHLAAPGLL RLVRKDAERI PVGKRRGQHT LPQEAINDKL IELAAAGKRV 310 320 330 340 350 360 LRLKGGDPFI FGRGGEEIEG LIEHGIPFQV VPAVTAAQGA AAYAGIPLTH RDHAQSCRFL 370 380 390 400 410 420 TGHRRHGALE LGQWAPFRSD ETLVVYMGLT HLETVSAQLQ AGGLPPDQPA AAVDQATTPA 430 440 450 460 470 480 QRVITAPLAE LPERVRTARL QGPALIVVGA TVTLQPQLGW YHSSPNAEPA FPEHGCLRGE 490 PRPTRHPAPA DTEQA

References

[1]

"Complete sequence of Halorhodospira halophila SL1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000544 Genomic DNA. Translation: ABM62697.1.
RefSeq	YP_001003499.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4710778.
GenomeReviews	Gene locus Hhal_1933 in contig CP000544_GR.
KEGG	hha:Hhal_1933.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1WYD5. DYAQSAV.
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR000878. 4pyrrol_Mease. IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR016040. NAD(P)-bd_dom. IPR019478. Sirohaem_synthase_dimer_dom. IPR006367. Sirohaem_synthase_N. 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	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. False negative. PS00840. SUMT_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG2_HALHL

Accession

Primary (citable) accession number: A1WYD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 22 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)