Q9AGW2 (SODC_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	sodC
Ordered Locus Names:	MAP_3921

Organism

Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]

Taxonomic identifier

262316 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) › Mycobacterium avium › Mycobacterium paratuberculosis

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. May play a role in favoring mycobacterial survival in phagocytes By similarity.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit Potential. Binds 1 zinc ion per subunit Potential.
Subcellular location	Cell membrane; Lipid-anchor By similarity.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.
Caution	Lacks three conserved histidine residues that bind copper and zinc.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond Lipoprotein Palmitate
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase 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
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 227	208	Superoxide dismutase [Cu-Zn]		PRO_0000032839
Sites
	Metal binding	103	1	Copper; catalytic By similarity
	Metal binding	105	1	Copper; catalytic By similarity
	Metal binding	145	1	Zinc; structural By similarity
	Metal binding	182	1	Copper; catalytic By similarity
Amino acid modifications
	Lipidation	20	1	N-palmitoyl cysteine Potential
	Lipidation	20	1	S-diacylglycerol cysteine Potential
	Disulfide bond	110 ↔ 221		By similarity
Experimental info
	Sequence conflict	16 – 18	3	ALG → GC in AAK20038. Ref.1
	Sequence conflict	186	1	D → N in AAK20038. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9AGW2 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: E5EE567880C00D5E	FASTA	227	22,466
	10 20 30 40 50 60 MPKLLPPVVL AGCVVALGAC SSPQHASSLP GTTPAVWTGS PSPSGAGAAE AAPAAAPSIT 70 80 90 100 110 120 THLKAPDGTQ VATAKFEFSN GYATVTIETT ANGVLTPGFH GVHIHKVGKC EPSSVAPTGG 130 140 150 160 170 180 APGDFLSAGG HFQAPGHTGE PASGDLTSLQ VRKDGSGTLV TTTDAFTMED LLGGRKTAII 190 200 210 220 IHAGADNFAN IPAERYNQTN GTPGPDEMTM STGDAGKRVA CGVIGAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, cloning and expression of sodC from an alkaline phosphatase gene fusion library of Mycobacterium avium subspecies paratuberculosis." Dupont C., Murray A. Microbios 106:7-19(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis." Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF326234 Genomic DNA. Translation: AAK20038.1. AE016958 Genomic DNA. Translation: AAS06471.1.
RefSeq	NP_962855.1. NC_002944.2.
3D structure databases
ProteinModelPortal	Q9AGW2.
SMR	Q9AGW2. Positions 58-227.
ModBase	Search...
Protein-protein interaction databases
STRING	262316.MAP3921.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS06471; AAS06471; MAP_3921.
GeneID	2719337.
KEGG	mpa:MAP3921.
PATRIC	18000734. VBIMycAvi108102_4173.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2032.
KO	K04565.
OMA	YNQTNGT.
ProtClustDB	CLSK790516.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024136. SOD_Cu/Zn. IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit. PTHR10003:SF11. PTHR10003:SF11. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. PS00087. SOD_CU_ZN_1. False negative. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC_MYCPA

Accession

Primary (citable) accession number: Q9AGW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	March 15, 2004
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program