Q1LTP4 (CYSG_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Siroheme synthase

Including the following 3 domains:

1. 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. Precorrin-2 dehydrogenase
   EC=1.3.1.76
3. Sirohydrochlorin ferrochelatase
   EC=4.99.1.4

Gene names

Name:	cysG
Ordered Locus Names:	BCI_0215

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	462 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: UniProtKB-KW siroheme biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro precorrin-2 dehydrogenase activity Inferred from electronic annotation. Source: EC sirohydrochlorin ferrochelatase activity Inferred from electronic annotation. Source: EC uroporphyrin-III C-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Siroheme synthase HAMAP MF_01646		PRO_0000330493
Regions
	Region	217 – 458	242	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	Q1LTP4 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: EDBB85CE0EFAFA5B	FASTA	462	51,049
	10 20 30 40 50 60 MEYLPLFANL RQRTVLVVGG GNVAARKIQL LMRTGAHIKV VADDLCPELA RIVNKKDINW 70 80 90 100 110 120 IGKLFEPAML DEVFLVIAAT NNTKLNALVY KCAEKRHIFA NIVDKQSYCS FIFPSIVDRS 130 140 150 160 170 180 PIVVAISSSG KAPVLARILR EKIETILPMF IGPMATLVGT WRNRIKQHIH NIAWRRRFWE 190 200 210 220 230 240 TILNGRFAHL ISQGKWEHAE KEIESQLYHY QSPIGNVALV GAGPGDSGLL TLRGLQLMQQ 250 260 270 280 290 300 ADIVLYDYLV SPEILDLVRR DADRIYVGKQ AGKHSMPQAE INSLLVKLAL QGKNVVRLKG 310 320 330 340 350 360 GDPFIFGRGG EELQAVAAAG ISFQVVPGIT AASGATAYAG IPLTHREYAH SVIFITGHQC 370 380 390 400 410 420 DDSSNYLNWS LLARSNQTLV IYMGVIQAAV IKKKLLAHGR ALQTPVAVIS RGTLKDQSVI 430 440 450 460 IGTLEQLEML TIQALSPTLL IIGEVVKISC EINWFGKIIK EQ

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF14343.1.
RefSeq	YP_588670.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LTP4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LTP4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056195.
GenomeReviews	Gene locus BCI_0215 in contig CP000238_GR.
KEGG	bci:BCI_0215.
PATRIC	21073929. VBIBauCic75062_0203.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0007.
HOGENOM	HBG730212.
OMA	HIFANIV.
PhylomeDB	Q1LTP4.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0215-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. IPR012409. Sirohaem_synth. 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. G3DSA:1.10.8.210. Sirohaem_synthase_dimer_dom. 1 hit.
KO	K02302.
Pfam	PF10414. CysG_dimeriser. 1 hit. PF00590. TP_methylase. 1 hit. [Graphical view]
PIRSF	PIRSF036426. Sirohaem_synth. 1 hit.
SUPFAM	SSF53790. Cor/por_Metransf. 1 hit.
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_BAUCH

Accession

Primary (citable) accession number: Q1LTP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program