ID   L9XI23_9EURY            Unreviewed;       501 AA.
AC   L9XI23;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Chlorite dismutase {ECO:0000313|EMBL:ELY61394.1};
GN   ORFNames=C491_01012 {ECO:0000313|EMBL:ELY61394.1};
OS   Natronococcus amylolyticus DSM 10524.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=1227497 {ECO:0000313|EMBL:ELY61394.1, ECO:0000313|Proteomes:UP000011688};
RN   [1] {ECO:0000313|EMBL:ELY61394.1, ECO:0000313|Proteomes:UP000011688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10524 {ECO:0000313|EMBL:ELY61394.1,
RC   ECO:0000313|Proteomes:UP000011688};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY61394.1}.
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DR   EMBL; AOIB01000005; ELY61394.1; -; Genomic_DNA.
DR   RefSeq; WP_005553074.1; NZ_AOIB01000005.1.
DR   AlphaFoldDB; L9XI23; -.
DR   STRING; 1227497.C491_01012; -.
DR   PATRIC; fig|1227497.3.peg.213; -.
DR   eggNOG; arCOG03031; Archaea.
DR   eggNOG; arCOG05403; Archaea.
DR   OrthoDB; 8690at2157; -.
DR   Proteomes; UP000011688; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR010644; ChdC/CLD.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   PANTHER; PTHR36843:SF1; COPROHEME DECARBOXYLASE; 1.
DR   PANTHER; PTHR36843; HEME-DEPENDENT PEROXIDASE YWFI-RELATED; 1.
DR   Pfam; PF03992; ABM; 1.
DR   Pfam; PF06778; Chlor_dismutase; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 2.
DR   PROSITE; PS51725; ABM; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          411..499
FT                   /note="ABM"
FT                   /evidence="ECO:0000259|PROSITE:PS51725"
FT   REGION          259..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  56613 MW;  EDDDCD37DBA13F66 CRC64;
     MERRRPPQTE EGWYVLHDFR SIDWDAWRDA PERHRSSALE EGVDYLSAAE DAVDAEEGES
     ATFAMLGHKA DLLVLHLRPT LADIDALERG FEQTALAEYT ERADSYLSVT EVSGYMSEEF
     FEDDEEVEDT GMRRYIETRL KPTIPDSEFV SFYPMDKRRG DADNWYDLPF DERANHLSSH
     GEIGKEYAGR VTQIISGSIG LDDFEWGVTL FADDPTDVKD LLYEMRFDPS TSRFAEFGRF
     LSGRRFPPTQ LRAFLAGEPI PQDESDHGHN HGESTHGDSS GHHHGDSDGS DGHHGGDDGD
     DDESVRSELE EMGVYAGQPH GEDVHAVVLY SAADPEELYE EVDGLRTNFD HYDTHVKTAV
     YEPSELADEE SETAVVSLWE TERAANTAAG FLADLPEIVR QAGDDSDDSW GTMGMFYAVK
     PEHREDFIDT FEDAGALLAD MEGHRKTDLL ANLEDENDMF IASRWDSRED AMQFFRSDAF
     ADAVEFGRDV LEKRPRHVFL A
//