ID M2WWB3_9PSEU Unreviewed; 280 AA.
AC M2WWB3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:EME53031.1};
GN ORFNames=H074_31962 {ECO:0000313|EMBL:EME53031.1};
OS Amycolatopsis decaplanina DSM 44594.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME53031.1, ECO:0000313|Proteomes:UP000054226};
RN [1] {ECO:0000313|EMBL:EME53031.1, ECO:0000313|Proteomes:UP000054226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME53031.1,
RC ECO:0000313|Proteomes:UP000054226};
RX PubMed=23558534;
RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM 44594T.";
RL Genome Announc. 1:E0013813-E0013813(2013).
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007825}.
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:EME53031.1}.
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DR EMBL; AOHO01000074; EME53031.1; -; Genomic_DNA.
DR RefSeq; WP_007034193.1; NZ_AOHO01000074.1.
DR AlphaFoldDB; M2WWB3; -.
DR PATRIC; fig|1284240.4.peg.6516; -.
DR OrthoDB; 9800887at2; -.
DR Proteomes; UP000054226; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd12214; ChiA1_BD; 1.
DR CDD; cd00421; intradiol_dioxygenase; 1.
DR Gene3D; 2.60.130.10; Aromatic compound dioxygenase; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR33711:SF7; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14270)-RELATED; 1.
DR PANTHER; PTHR33711; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF49482; Aromatic compound dioxygenase; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:EME53031.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..280
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004028283"
FT DOMAIN 234..280
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 43..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 29594 MW; 13F24DDC86D6A4FB CRC64;
MDEENKLSRK TVLKAALAAG VAAPVALIGG PALARTTVAN GQAPELTPAC DDGDDPTPPQ
TEGPYFKPNS PQRTSLVTSG TPGTRLTVSG YVFGLGCLPI ARALLDFWQA DVNGAYDNVG
YTFRGHQFTN DQGAFSLSTI VPGLYPGRTR HIHVKVQAPG RPVLTTQLYF PNEPRNNTDT
IFDPRLLMTV RDVGTAKEAA FDFVLNVPQT PTSTSRPTST TPTTSTSTSN PPGGTTWAAG
TGYSAGARVT YSGSGYVCLQ AHTAQPGWEP PSTPALWRAE
//
