Siroheme synthase - Neisseria meningitidis serogroup A

Contribute

Send feedback

Read comments (?) or add your own

P57001 (CYSG_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Siroheme synthase

Including the following 3 domains:

Uroporphyrinogen-III C-methyltransferase
Short name=Urogen III methylase
EC=2.1.1.107
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name=UROM
Precorrin-2 dehydrogenase
EC=1.3.1.76
Sirohydrochlorin ferrochelatase
EC=4.99.1.4

Gene names

Name:	cysG
Ordered Locus Names:	NMA1367

Organism

Neisseria meningitidis serogroup A [Complete proteome] [HAMAP]

Taxonomic identifier

65699 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	486 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 – 486

486

Siroheme synthase HAMAP MF_01646

PRO_0000150381

Regions

Region

219 – 459

241

Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence

Length

Mass (Da)

Tools

P57001 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: F70D6A5F50FF23CF
Show »

FASTA

486

52,484

        10         20         30         40         50         60 
MNYFPIFANL AGRPVLVVGG GAVAARKISL LLKAGAEVRV AAKHLNAELS ALAAENKILW 

        70         80         90        100        110        120 
LAEEFRAEHI RTVFLIIAAS SDQALNRRVF HLAESCQKPV NVVDDRDHCS FIFPSVIDRN 

       130        140        150        160        170        180 
PVQIAVSSSG SAPVLARLLR ERLEALLPPS LGDMAEISGR WRDAVKGKLK SVTERRRFWE 

       190        200        210        220        230        240 
KQFNGRFAAL VKNRQNTLAE RELAGQLEQS RQNDQGGSVS LVGAGPGDAG LLTLKGLQEI 

       250        260        270        280        290        300 
QQADVVLYDA LVSDGILSLV RRDAERIFVG KRARGGRTPQ EDTNALMVRL AREGRRVVRL 

       310        320        330        340        350        360 
KGGDPFVFGR GGEELETLAR HQIPFSVVPG ITAAVGATAY AGIPLTHRDY AQSAVFVTGH 

       370        380        390        400        410        420 
RKADAPDIEW QTLARSRQTL VIYMGALKAA LIAERLQQHG RSPDTPAAVI SQGTLPAQKT 

       430        440        450        460        470        480 
ATGTLANLAE LAETAPNPAL IVIGEVVGLH EKLAWFGENA KKESNPAEHA YFALDGLGTG 


QEQQAA

« Hide

References

[1]

"Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491."
Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S.

Barrell B.G.
Nature 404:502-506(2000) [PubMed: 10761919] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z2491 / Serogroup A / Serotype 4A.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL157959 Genomic DNA. Translation: CAM08540.1.
PIR	A81906.
RefSeq	YP_002342721.1. NC_003116.1.
3D structure databases
ProteinModelPortal	P57001.
SMR	P57001. Positions 1-458.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000001219; EBNEIP00000001219; EBNEIG00000001219.
GeneID	907774.
GenomeReviews	Gene locus NMA1367 in contig AL157959_GR.
KEGG	nma:NMA1367.
PATRIC	20363765. VBINeiMen132687_1591.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000020161.
HOGENOM	HBG730212.
OMA	DYAQSAV.
ProtClustDB	CLSK877926.
Enzyme and pathway databases
BioCyc	NMEN122587:NMA1367-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_NEIMA

Accession

Primary (citable) accession number: P57001
Secondary accession number(s): A1IRZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents