ID Q8NR75_CORGL Unreviewed; 527 AA.
AC Q8NR75; Q6M5Z5;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Predicted hydrolases or acyltransferases (Alpha/beta hydrolase superfamily) {ECO:0000313|EMBL:BAB98571.1};
GN OrderedLocusNames=Cgl1178 {ECO:0000313|EMBL:BAB98571.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB98571.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; BA000036; BAB98571.1; -; Genomic_DNA.
DR RefSeq; NP_600404.1; NC_003450.3.
DR AlphaFoldDB; Q8NR75; -.
DR STRING; 196627.cg1332; -.
DR ESTHER; corgl-CGL1178; Tiancimycin-TnmK-Tripeptidase-HIP.
DR DNASU; 1019161; -.
DR KEGG; cgl:Cgl1178; -.
DR PATRIC; fig|196627.13.peg.1157; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_013364_3_2_11; -.
DR OrthoDB; 4447445at2; -.
DR BioCyc; CORYNE:G18NG-10751-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 Acyltransferase {ECO:0000313|EMBL:BAB98571.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAB98571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:BAB98571.1}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039579269"
FT DOMAIN 95..261
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 425..513
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 527 AA; 55955 MW; 962CA5DF8BF5406D CRC64;
MPRSTIKRVV AVLAASTALS PFLVSMPTAA AQENIRWEEC PPQVDIASAQ CGSIDVPMHY
SDPSLGDISV GFVKVPAQGE KHGTIFGNSG GPGGDAYSFF GSQSMNWPEA MYQNYDLVAV
QPRGMVGSTP VNCDNIAPGY DFLSLLTREG AFVKESCEIG TPGYTSSLTT DNTANDWERV
RQALGDDKIS IFGLSYGTYL GSVYATRYPQ HTDKVVLDSA MAPSLAWNGI MASQEQGYKN
SLNDFFTWVA ENNDTYGLGT TPLAVYQNWS NKIVAETGTN PTVAPPPAQV GDVPPAFAWA
GQAGADMMTA TNPTSVQLQG LATQLLNPGS NQSLSPLLNV TRAYIPQPST WPMLAGAISG
QTPIPDVTDT GDDPYVIESI NASVNMQRMV MCNENTVAPD PVAMARMAWT SMVTGDVFDI
YSVKFSSGQA CSGITPTSGR QPTDGSQLAV QPLLLQGTSD PQTPYWTHNE LADAMNAHVV
TVNGPGHGQS IGGTNQAIND IVVDYLRTGH TDATWVEGNT PTPITAG
//
