ID A0A1I0VNV8_9ACTN Unreviewed; 284 AA.
AC A0A1I0VNV8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05192575_101346 {ECO:0000313|EMBL:SFA78002.1};
OS Nocardioides alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=748909 {ECO:0000313|EMBL:SFA78002.1, ECO:0000313|Proteomes:UP000199113};
RN [1] {ECO:0000313|EMBL:SFA78002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFA78002.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOKC01000001; SFA78002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VNV8; -.
DR STRING; 748909.SAMN05192575_101346; -.
DR Proteomes; UP000199113; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ SEQUENCE 284 AA; 32151 MW; AA84622DAF9D9B87 CRC64;
MHVHAHPDDE SSKGAASTAK YVSEGVDVHV ATCTGGERGS VLNAKMDRPE VWENISEIRR
EEMHRARDIL GIRQDWLGFV DSGWPEGDPK PPLPEGCFAL VPLEEATERL VRLIREFRPH
VLTTYDERGG YPHPDHIRCH EVSVAAYAAA GDPEQFPDAG EPWQPMKLYY HHGWSWAKTN
ALHEAMLAHG LESPYTERLA TWEREADWDD RITTRVPCGD FFGVRDQALL AHATQIDPDG
MWFAIPREIQ QKVWPTEDYE LVESTVESTR PEDDLFAGIP IPAP
//
