ID D9WT37_9ACTN Unreviewed; 425 AA.
AC D9WT37;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=3-oxoadipate enol-lactonase {ECO:0000313|EMBL:EFL26258.1};
GN ORFNames=SSOG_05972 {ECO:0000313|EMBL:EFL26258.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL26258.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL26258.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL26258.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657754; EFL26258.1; -; Genomic_DNA.
DR AlphaFoldDB; D9WT37; -.
DR STRING; 457427.SSOG_05972; -.
DR HOGENOM; CLU_020336_54_1_11; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR Gene3D; 1.20.1290.10; AhpD-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR029032; AhpD-like.
DR InterPro; IPR003779; CMD-like.
DR InterPro; IPR012788; Decarb_PcaC.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR NCBIfam; TIGR02425; decarb_PcaC; 1.
DR PANTHER; PTHR33570; 4-CARBOXYMUCONOLACTONE DECARBOXYLASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR33570:SF2; CARBOXYMUCONOLACTONE DECARBOXYLASE-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR Pfam; PF02627; CMD; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF69118; AhpD-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
FT DOMAIN 47..164
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 228..292
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT DOMAIN 329..411
FT /note="Carboxymuconolactone decarboxylase-like"
FT /evidence="ECO:0000259|Pfam:PF02627"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 45174 MW; BE7D05A505D896C2 CRC64;
MGDKHPRTGT GTRIHTPSHP TNHPPESHPV SHTHELNATL DGPATAPPLI LGPSIGTSLA
VWEPQLPALA RTHRTLRWDL PGHGGSPATA LPNDGSATIA DLAALVLNLA DAHNWDRFSY
AGISIGGAVG LYLAAHHPDR VSSLAIVCSS AHFAEPSVWR DRAKLVREQG TEAMVASRPG
LWFSHEFADT DRGRALLQDL RDTDRAGYAA CCDVLADYDV RDVLPSITAP TLVVAGRDDP
ATPPPHAREI ADATPGASLV EVAHAAHLAG AERPEAVTSA LVTHFANPDT KAPTDDTTRH
AAGMAVRRAV LGDAHVDRAV ARTTPFTARF QDFITRYAWG EIWTGDGLDR RMRSAVTLTA
LIAHGHDAEL AMHVRSALTN GLTRDEIGEV LLQSAIYCGV PAANSAFATA QRVFDEIDTE
ASKGS
//
