ID E3ECK9_PAEPS Unreviewed; 459 AA.
AC E3ECK9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN Name=sodF {ECO:0000313|EMBL:ADO54781.1};
GN ORFNames=PPSC2_03965 {ECO:0000313|EMBL:ADO54781.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO54781.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO54781.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO54781.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002213; ADO54781.1; -; Genomic_DNA.
DR RefSeq; WP_013369417.1; NC_014622.2.
DR AlphaFoldDB; E3ECK9; -.
DR STRING; 1406.LK13_16770; -.
DR KEGG; ppm:PPSC2_03965; -.
DR PATRIC; fig|886882.15.peg.788; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_5_2_9; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000006868; 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 Gene3D; 1.20.1260.120; Protein of unknown function DUF2935; 1.
DR InterPro; IPR021328; CotB-like.
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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR Pfam; PF11155; DUF2935; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF158430; Bacillus cereus metalloprotein-like; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT DOMAIN 258..338
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 345..447
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT REGION 74..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 52143 MW; 62F32FC3129246EC CRC64;
MLSTYGSFLP LRVLEEIRHW KQQESWHVEV IKSATEGLEP AYVRLLDDWR TVFEQTERAA
IELLEEQRSA LDPVEQAWQH QEKKASSAPQ AHTHQLDESS AHSRGSDASA TGEKPLSESG
LNSQPASQEL NRRLDDLLQT ANRQSQEYVR QLGLLTEHSH ALRQQPKSAG VVIHAAHESQ
YFLISTTPFQ EPGSIARATG LYHVAAEGED YPEQAFRERH ASMRGEGSGA TKGVQSGQTQ
PSAAEKSLVG RPVPIGGHRL PPLPYPYNAL EPYIDEKTMR IHHNKHHLSY VNDLNKAEKK
LEEARKTGDF DLVKHWEREL AFNGAGHYLH TLFWTIMSPQ GGGNPSGPLA EQIKKDFGSY
DAFKKQFSSA AEKVEGGGWA ILVWSPRSGR LEILQAEKHQ NLTQWESIPL LAIDVWEHAY
YLKHQAERNK YIEDWWHVVN WPEVEARYAQ ASKLRWQPF
//