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Database: UniProt
Entry: Q2WAU6_MAGSA
LinkDB: Q2WAU6_MAGSA
Original site: Q2WAU6_MAGSA 
ID   Q2WAU6_MAGSA            Unreviewed;       255 AA.
AC   Q2WAU6;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Uncharacterized conserved protein {ECO:0000313|EMBL:BAE49029.1};
GN   OrderedLocusNames=amb0225 {ECO:0000313|EMBL:BAE49029.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE49029.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE49029.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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DR   EMBL; AP007255; BAE49029.1; -; Genomic_DNA.
DR   RefSeq; WP_011382672.1; NC_007626.1.
DR   AlphaFoldDB; Q2WAU6; -.
DR   STRING; 342108.amb0225; -.
DR   KEGG; mag:amb0225; -.
DR   HOGENOM; CLU_046582_2_1_5; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   Gene3D; 3.40.830.10; LigB-like; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR   SUPFAM; SSF53213; LigB-like; 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:UP000007058};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..254
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   255 AA;  27790 MW;  935A07FD9D15CB19 CRC64;
     MDVTTLFLSH GSPMMVLEDT PTRRFLKELG RRLPRPPAVI AVSAHWQTAE PVLGFAAWPD
     KINDIYGFPP ELYQLAYAPP GAPEVAARAA DRLGAACRRD PGAGIDHSIW SVMSLMWPEA
     DVPVVPMSVQ PEAGASHHYF LGRRLAPLVA EGVLVIGSGA ATHNLEDYFR RKTTEAVEPA
     VVEFTDWLAA TAERGDVAAL LDYRVRAPHA LRNHPTEEHL LPLFVALGAS AHGEAVRLHH
     DVDSGVLAMD AYGFR
//
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