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Database: UniProt
Entry: A0A1H9M382_9PSEU
LinkDB: A0A1H9M382_9PSEU
Original site: A0A1H9M382_9PSEU 
ID   A0A1H9M382_9PSEU        Unreviewed;       510 AA.
AC   A0A1H9M382;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha/beta hydrolase fold {ECO:0000313|EMBL:SER18091.1};
GN   ORFNames=SAMN04488000_106402 {ECO:0000313|EMBL:SER18091.1};
OS   Lentzea albida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=65499 {ECO:0000313|EMBL:SER18091.1, ECO:0000313|Proteomes:UP000199503};
RN   [1] {ECO:0000313|EMBL:SER18091.1, ECO:0000313|Proteomes:UP000199503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44437 {ECO:0000313|EMBL:SER18091.1,
RC   ECO:0000313|Proteomes:UP000199503};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOFV01000006; SER18091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9M382; -.
DR   STRING; 65499.SAMN04488000_106402; -.
DR   OrthoDB; 4006962at2; -.
DR   Proteomes; UP000199503; Unassembled WGS sequence.
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; IPR000073; AB_hydrolase_1.
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; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SER18091.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..510
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011795196"
FT   DOMAIN          88..281
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          392..485
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   510 AA;  55663 MW;  D38ADCB42F96468A CRC64;
     MQPMVRVFGA AIASSALVLG ASQVAIAAPE GQPEFNVGAV DWKPCEEVPA VECGFLELPV
     DYAKPRGEKF QLAVSRRKAN DPAQRIGAMV INPGGPGGSG VDFSFGADRY FSKEIVDKFD
     IIGFDPRGVA RSAPIKCSAE LLQKTPSSYP KTKAEFDALV VFNKELRADC EKQTGAIFNH
     ASTAEVAQDI DSIRRALGEK KINYYGISYG TIMGQHYAEK FGKNIRAMII DSNMDHSLGT
     KAFLDSEART AEDSFNEWIK WNDRTTSSPF HGQDLRKIWK DLLAKAERGE VPAPWDPAAK
     LTPEDLGGGV VSMAYGPNWK GFADQIKQII DGTQAPKSAF SAFAAEETFP NPFPGIFCND
     YNLRVSSWGE YQALTKSEYR IAPNTRGSSL GHGAMMGCVG FPKATNPQRT LKIKNSPKIL
     LTNAKHDPAT AYEWAVNAHR QTRDTTVFVT YEGWGHGVYD RSECTLKINN EYLVSLKLPR
     NGTSCAAVEP AETSVLSVKP RVPAGPFSIA
//
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