F0MR64 (F0MR64_NEIMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn] RuleBase RU000393
EC=1.15.1.1 RuleBase RU000393

Gene names

Ordered Locus Names:

NMBM01240149_0758 EMBL ADY97349.1

Organism

Neisseria meningitidis serogroup B (strain M01-240149) [Complete proteome] [HAMAP]

Taxonomic identifier

935591 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › Neisseria meningitidis

Protein attributes

Sequence length	186 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. RuleBase RU000393
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000393
Cofactor	Binds 1 copper ion per subunit By similarity. RuleBase RU000393 Binds 1 zinc ion per subunit By similarity. RuleBase RU000393
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family. RuleBase RU000393

Ontologies

Keywords
Ligand	Copper RuleBase RU000393 Metal-binding RuleBase RU000393 Zinc RuleBase RU000393
Molecular function	Oxidoreductase RuleBase RU000393
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	F0MR64 [UniParc]. Last modified May 3, 2011. Version 1. Checksum: 6499049BFAC3427C	FASTA	186	19,520
	10 20 30 40 50 60 MNMKTLLALA VSAVCSVGVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV GTVTITESNY 70 80 90 100 110 120 GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG AGGHWDPKGA KQHGYPWQDD 130 140 150 160 170 180 AHLGDLPALT VLHDGTATNP VLAPRLKHLD DVRGHSIMIH TGGDNHSDHP APLGGGGPRM ACGVIK

References

[1]

"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination." Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D. Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: M01-240149 EMBL ADY97349.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002421 Genomic DNA. Translation: ADY97349.1.
RefSeq	YP_005895560.1. NC_017514.1.
3D structure databases
ProteinModelPortal	F0MR64.
SMR	F0MR64. Positions 32-186.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADY97349; ADY97349; NMBM01240149_0758.
GeneID	12412438.
KEGG	nmm:NMBM01240149_0758.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K04565.
OMA	NTNSHQG.
Enzyme and pathway databases
BioCyc	NMEN935591:GLHR-757-MONOMER.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F0MR64_NEIMM

Accession

Primary (citable) accession number: F0MR64

Entry history

Integrated into UniProtKB/TrEMBL:	May 3, 2011
Last sequence update:	May 3, 2011
Last modified:	May 29, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)