Reviewed, UniProtKB/Swiss-Prot Q21K21 (CYSG_SACD2)

Names and origin

Protein names

Recommended name:
    Siroheme synthase
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:	cysG
Ordered Locus Names:	Sde_1698

Organism

Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]

Taxonomic identifier

203122 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Saccharophagus

Protein attributes

Sequence length	458 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.

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 – 458	458	Siroheme synthase		PRO_0000330551
Regions
	Region	218 – 458	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q21K21-1 [UniParc]. Last modified April 18, 2006. Version 1. Checksum: 00C40A4EBBA40706	FASTA	458	50,119
	10 20 30 40 50 60 MDYLPLFFDL KAKPCLIVGG GTIATRKARL LHKAGAKLHV VAPKVSEELE KLVAASNGKV 70 80 90 100 110 120 FKQEYDQTFL DDVILVISAT DIDAVNSVVA ADCHAIKLPV NVVDSPALCS VIMPAIIDRS 130 140 150 160 170 180 PLIIGVTSGG EAPVLARRVR SMLESSIPAA YGQLAQLASK FRQRAKDVFE NGDLRRRFWE 190 200 210 220 230 240 NILNGPIAEK VLGGNLAAAE QLIEAQLDSA SVEKTGEVYL VGAGPGDPDL LTFKALRLMQ 250 260 270 280 290 300 QAEVVLYDRL VSEPILEMTR RDAERIYVGK KRAEHAVPQQ KINQMLLELA QQGKRVLRLK 310 320 330 340 350 360 GGDPFIFGRG GEEIDLLAEH KIPFQVVPGI TAASGCASYS GIPLTHRDYS QSVRFITGHL 370 380 390 400 410 420 QEGKENFRWS EFVDKQQTLV FYMGLAGLET ICSKLIEYGK SPSTPAALIE RGTLPEQRVH 430 440 450 VSDLAGLAAK IEGLDVHAPT LLIIGDVVRC HEKLNWYK

References

[1]

"Complete sequence of Saccharophagus degradans 2-40." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Kyrpides N., Lykidis A., Richardson P., Weiner R. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000282 Genomic DNA. Translation: ABD80958.1.
RefSeq	YP_527170.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3966485.
GenomeReviews	Gene locus Sde_1698 in contig CP000282_GR.
KEGG	sde:Sde_1698.
NMPDR	fig|203122.1.peg.4259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q21K21.
Enzyme and pathway databases
BioCyc	SDEG203122:SDE_1698-MON.
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. False negative. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG_SACD2

Accession

Primary (citable) accession number: Q21K21

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 18, 2006
Last modified:	November 25, 2008
This is version 25 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)