ID A0A1D8G627_9ACTN Unreviewed; 526 AA.
AC A0A1D8G627;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carboxylesterase A {ECO:0000313|EMBL:AOT60916.1};
DE EC=3.1.1.- {ECO:0000313|EMBL:AOT60916.1};
GN Name=caeA_2 {ECO:0000313|EMBL:AOT60916.1};
GN ORFNames=A4G23_03791 {ECO:0000313|EMBL:AOT60916.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT60916.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT60916.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT60916.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP017316; AOT60916.1; -; Genomic_DNA.
DR RefSeq; WP_031129855.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8G627; -.
DR STRING; 285473.A4G23_03791; -.
DR KEGG; srn:A4G23_03791; -.
DR PATRIC; fig|285473.5.peg.3973; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000095349; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AOT60916.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..526
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038477781"
FT DOMAIN 420..524
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 33..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 54667 MW; 5B0D6611119AFAAA CRC64;
MTKRVRVRAV AAAATAALVA GVVAGCQGDG AAGSAGAGAA PSAGGAAPVR PGSSAGMPDL
PAALTGQKPR WGACEAPEGG EDPGEGWRCA TVKVPLDYRE PDGETLAVAL IRKEAREKKG
RIGSLLFNFG GPGASGVEML PGFAPGYEAL NARYDLVGFD PRGVGGSSAV VCRSDEEQAA
AEKRIDLTPD TPAEEAAYLK DGADFGAGCA RRSGKLIPHV TTGNTARDMD VIRHVLGDDR
LYYFGISYGT QLGAAYAHLF PKHTGRTVLD AVVDPTADSL GHARHQTTGF QRALNNYLAS
TGEDAAEGTA RIARLLDRLD ERPLPTSGDR KLTEGLALTG IVLPLYSESS WPLLTEALRE
AEGGRGDALL RLADMYNERD EDGRYGTDSH SQRAISCADT DQRPTAAEAK ALLPEFRRIS
PVFGEFLAWD TAGWCANWPV KGEGGGQDVS APGAQPILVV GTTGDPATPY EGARKMADGL
GKGVGVLVTN KGEGHGAYGT SGCVTRTVDD YLLRGKVPAD GTTCSS
//