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Database: UniProt
Entry: C1D8B1_LARHH
LinkDB: C1D8B1_LARHH
Original site: C1D8B1_LARHH 
ID   C1D8B1_LARHH            Unreviewed;       196 AA.
AC   C1D8B1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   Name=sodB1 {ECO:0000313|EMBL:ACO74701.1};
GN   OrderedLocusNames=LHK_01716 {ECO:0000313|EMBL:ACO74701.1};
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO74701.1, ECO:0000313|Proteomes:UP000002010};
RN   [1] {ECO:0000313|EMBL:ACO74701.1, ECO:0000313|Proteomes:UP000002010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9 {ECO:0000313|EMBL:ACO74701.1,
RC   ECO:0000313|Proteomes:UP000002010};
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA   Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA   Pallen M.J., Lok S., Yuen K.Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001154; ACO74701.1; -; Genomic_DNA.
DR   RefSeq; WP_012697187.1; NC_012559.1.
DR   AlphaFoldDB; C1D8B1; -.
DR   STRING; 557598.LHK_01716; -.
DR   GeneID; 75108856; -.
DR   KEGG; lhk:LHK_01716; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_4; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000002010; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002010}.
FT   DOMAIN          2..79
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          92..193
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         74
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   196 AA;  21915 MW;  5F8B160ABF2ED399 CRC64;
     MEHKLPELPY ALDALVPFMS RETLEYHYGK HHQTYITNLN NLIKGTEFEN APLETIVKQS
     SGGVFNNAAQ TWNHTFFWFG FAPNASGEAR LPSGALASAI DAKWGSLEEF KKAFNAVAAG
     TFGSGWAWLV KKADGSLDLV STSNAATPLT TDATPLLTCD VWEHAYYIDY RNSRPNYLEN
     FWKLVDWNVV AERFAA
//
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