ID A0A1T5IBU7_9MICO Unreviewed; 309 AA.
AC A0A1T5IBU7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Mycothiol S-conjugate amidase {ECO:0000256|HAMAP-Rule:MF_01482};
DE EC=3.5.1.115 {ECO:0000256|HAMAP-Rule:MF_01482};
GN Name=mca {ECO:0000256|HAMAP-Rule:MF_01482};
GN ORFNames=SAMN04324258_0307 {ECO:0000313|EMBL:SKC36671.1};
OS Krasilnikoviella flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Krasilnikoviella.
OX NCBI_TaxID=526729 {ECO:0000313|EMBL:SKC36671.1, ECO:0000313|Proteomes:UP000189777};
RN [1] {ECO:0000313|EMBL:SKC36671.1, ECO:0000313|Proteomes:UP000189777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21481 {ECO:0000313|EMBL:SKC36671.1,
RC ECO:0000313|Proteomes:UP000189777};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-
CC conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine
CC conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH
CC precursor. Involved in MSH-dependent detoxification of a number of
CC alkylating agents and antibiotics. {ECO:0000256|HAMAP-Rule:MF_01482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-
CC alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate;
CC Xref=Rhea:RHEA:36543, ChEBI:CHEBI:15377, ChEBI:CHEBI:58718,
CC ChEBI:CHEBI:58886, ChEBI:CHEBI:59633; EC=3.5.1.115;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01482};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01482};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01482};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01482}.
CC -!- SIMILARITY: Belongs to the MshB deacetylase family. Mca subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01482}.
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DR EMBL; FUZQ01000001; SKC36671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5IBU7; -.
DR STRING; 526729.SAMN04324258_0307; -.
DR Proteomes; UP000189777; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010126; P:mycothiol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010127; P:mycothiol-dependent detoxification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10320; LmbE-like; 1.
DR HAMAP; MF_01482; Mca; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR InterPro; IPR017811; Mca.
DR NCBIfam; TIGR03446; mycothiol_Mca; 1.
DR PANTHER; PTHR12993:SF32; MYCOTHIOL S-CONJUGATE AMIDASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01482};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01482};
KW Reference proteome {ECO:0000313|Proteomes:UP000189777};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ SEQUENCE 309 AA; 33348 MW; DEEEB6118B663225 CRC64;
MSSASSAPPA APSEPLRLMA VHAHPDDESS KGAATTARYA AEGVEVLVVT CTGGERGDVL
NPSFEVPAGH EFETIEGRRA VRRLEMAAAA EALGVRQTWL GFVDSGLPEG DPLPPLPEGS
FGLVPPAEAA APLVELVREF RPHVITTYDP SGGYPHPDHI KCHEVAVEAY HAAGDGSRYV
VEGGAEPWEP LKLYYNHGFS MARMRAVHEA MQGAGLESPF GDWIESRTAR EIPEREATTH
VAVADFFTQR DSALVAHASQ IDPDGFFFAV PRDLEADVWP TEEYELADSR VPTALPEDDL
FAGVREGDR
//
