Reviewed, UniProtKB/Swiss-Prot Q5FP95 (CYSG_GLUOX)

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:	GOX2065

Organism

Gluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP]

Taxonomic identifier

442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
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. HAMAP MF_01646
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 – 473	473	Siroheme synthase HAMAP MF_01646		PRO_0000330514
Regions
	Region	235 – 473	239	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	Q5FP95-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: D03C0C346C837C48	FASTA	473	51,101
	10 20 30 40 50 60 MNTQPHHSSP DSPQDGGWFP ISIRLSGARV LLVGGGEIAV NKGRLLLDHG ARIDVLAEKL 70 80 90 100 110 120 HPAVQGWVEN GRVRHVGERA DEAVLRRLLP GCRLVYAATD SRDTNRQVAA LADELNIPVC 130 140 150 160 170 180 AVDDPGPSSF ITPAQVRRGM VRVAVSTGGA APVLARRLRE QIETLLPEGT GRLATYMQSR 190 200 210 220 230 240 RAFVSGRYPN VQDRKRIWED FLDGPGAEAA RSGDESRADA RLEVLLDGER KSGEVWLVGA 250 260 270 280 290 300 GPGDPDLLTL KALHLMQNAD SVLYDNLVSP ALLDMVRRDA ELVFVGKQRD RHALPQDEIN 310 320 330 340 350 360 REMVRRAQGG ERVLRLKGGD PFIFGRGGEE IEALVEAGVA FRLVPGISAA NGCAAYSGIP 370 380 390 400 410 420 LTHRDCAQAC LFVTGHAKAD GVLDLPWDDM ADRRQTVVIY MGISTLPQLA AGLLGKGLPA 430 440 450 460 470 DWPVAIVERG TQPRQRVFTG TLSTIAQQAA EAQVKSPALV IVGQVVRHRV VSP

References

[1]

"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans." Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U. Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 621H.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000009 Genomic DNA. Translation: AAW61801.1.
RefSeq	YP_192457.1.
3D structure databases
HSSP	HSSP built from PDB template 1PJS based on UniProtKB P25924.
SMR	Q5FP95. Positions 17-469.
ModBase	Search...
Genome annotation databases
GeneID	3248247.
GenomeReviews	Gene locus GOX2065 in contig CP000009_GR.
KEGG	gox:GOX2065.
NMPDR	fig|290633.1.peg.2002.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG730212.
OMA	MCRRDAE.
Enzyme and pathway databases
BioCyc	GOXY290633:GOX2065-MONOMER.
Family and domain databases
HAMAP	MF_01646. Siroheme_synth. [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. 1 hit. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG_GLUOX

Accession

Primary (citable) accession number: Q5FP95

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	March 1, 2005
Last modified:	February 9, 2010
This is version 34 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)