P20379 (SODC_CAUCR) 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:	CC_1579

Organism

Caulobacter crescentus (Caulobacter vibrioides)

Taxonomic identifier

155892 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. May function against extracytoplasmic toxic oxygen species.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space 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 – 23	23
	Chain	24 – 174	151	Superoxide dismutase [Cu-Zn]		PRO_0000032823
Sites
	Metal binding	68	1	Copper; catalytic By similarity
	Metal binding	70	1	Copper; catalytic By similarity
	Metal binding	86	1	Copper; catalytic By similarity
	Metal binding	86	1	Zinc; structural By similarity
	Metal binding	95	1	Zinc; structural By similarity
	Metal binding	104	1	Zinc; structural By similarity
	Metal binding	107	1	Zinc; structural By similarity
	Metal binding	150	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	75 ↔ 170		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20379 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: F3B3C79EF3E3642C	FASTA	174	17,100
	10 20 30 40 50 60 MIRLSAAAAL GLAAALAASP ALAQTSATAV VKAGDGKDAG AVTVTEAPHG VLLKLELKGL 70 80 90 100 110 120 TPGWHAAHFH EKGDCGTPDF KSAGAHVHTA ATTVHGLLNP DANDSGDLPN IFAAADGAAT 130 140 150 160 170 AEIYSPLVSL KGAGGRPALL DADGSSIVVH ANPDDHKTQP IGGAGARVAC GVIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme." Steinman H.M., Ely B. J. Bacteriol. 172:2901-2910(1990) [PubMed: 2345128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 19089 / CB15.
[2]	"Complete genome sequence of Caulobacter crescentus." Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J. , Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001) [PubMed: 11259647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19089 / CB15.
[3]	"Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme." Steinman H.M. J. Biol. Chem. 257:10283-10293(1982) [PubMed: 7050107] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Strain: ATCC 19089 / CB15.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55259 Genomic DNA. Translation: AAA23054.1. AE005673 Genomic DNA. Translation: AAK23558.1.
PIR	A35383.
RefSeq	NP_420390.1. NC_002696.2.
3D structure databases
ProteinModelPortal	P20379.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	941805.
GenomeReviews	Gene locus CC_1579 in contig AE005673_GR.
KEGG	ccr:CC_1579.
NMPDR	fig|190650.1.peg.1570.
PATRIC	21300180. VBICauCre124313_1607.
TIGR	CC_1579.
Phylogenomic databases
HOGENOM	HBG609879.
OMA	NTNSHQG.
ProtClustDB	CLSK890487.
Family and domain databases
InterPro	IPR024136. SOD_Cu/Zn. IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KO	K04565.
PANTHER	PTHR10003:SF11. PTHR10003:SF11. 1 hit. PTHR10003. SOD_Cu_Zn. 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

SODC_CAUCR

Accession

Primary (citable) accession number: P20379

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program