SODC_HAEIF
ID SODC_HAEIF Reviewed; 187 AA.
AC P25841;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Superoxide dismutase [Cu-Zn]-like;
DE Flags: Precursor;
GN Name=sodC;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NCTC 8468 / Serotype B;
RX PubMed=1938942; DOI=10.1128/jb.173.23.7449-7457.1991;
RA Kroll J.S., Langford P.R., Loynds B.M.;
RT "Copper-zinc superoxide dismutase of Haemophilus influenzae and H.
RT parainfluenzae.";
RL J. Bacteriol. 173:7449-7457(1991).
CC -!- FUNCTION: This protein lacks enzymatic activity (probably because of
CC the presence of a tyrosine instead of a histidine at residue 82).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M84012; AAA24953.1; -; mRNA.
DR PIR; A41654; A41654.
DR AlphaFoldDB; P25841; -.
DR SMR; P25841; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..187
FT /note="Superoxide dismutase [Cu-Zn]-like"
FT /id="PRO_0000032829"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT SITE 82
FT /note="Ancestral copper-binding site"
FT DISULFID 87..183
FT /evidence="ECO:0000250"
SQ SEQUENCE 187 AA; 19536 MW; 3EE95EFFD52425B3 CRC64;
MMKMKTLLAL AISGICAAGV ANAHDHMAKP AGPSIEVKVQ QLDPANGNKD VGTVTITESN
YGLVFTPNLQ GLAEGLHGFH IYENPSCEPK EKDGKLIAGL AAGGHWDSKG AKQHGYPWQD
DAHLGDLPAL TVLHDGTATN PVLAPRLKKL DEVRGHSIMI HAGGDNHSDH PAPLGGGGPR
MACGVIK
