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Database: UniProt
Entry: A0A1H5QUZ2_9PSEU
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ID   A0A1H5QUZ2_9PSEU        Unreviewed;       308 AA.
AC   A0A1H5QUZ2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE            Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE            EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068};
DE   AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase {ECO:0000256|HAMAP-Rule:MF_00068};
DE   AltName: Full=N-acetylmuramic acid 6-phosphate lyase {ECO:0000256|HAMAP-Rule:MF_00068};
GN   Name=murQ {ECO:0000256|HAMAP-Rule:MF_00068};
GN   ORFNames=SAMN05421837_104565 {ECO:0000313|EMBL:SEF29158.1};
OS   Amycolatopsis pretoriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF29158.1, ECO:0000313|Proteomes:UP000198878};
RN   [1] {ECO:0000313|EMBL:SEF29158.1, ECO:0000313|Proteomes:UP000198878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF29158.1,
RC   ECO:0000313|Proteomes:UP000198878};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether
CC       substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-
CC       lactate. {ECO:0000256|HAMAP-Rule:MF_00068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-
CC         acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:26410,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16004, ChEBI:CHEBI:57513,
CC         ChEBI:CHEBI:58722; EC=4.2.1.126; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00068};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00068}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068}.
CC   -!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is
CC       suggested for the cleavage of the lactyl ether bond of MurNAc 6-
CC       phosphate, with the formation of an alpha,beta-unsaturated aldehyde
CC       intermediate with (E)-stereochemistry, followed by the syn addition of
CC       water to give product. {ECO:0000256|HAMAP-Rule:MF_00068}.
CC   -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00068}.
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DR   EMBL; FNUJ01000004; SEF29158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5QUZ2; -.
DR   STRING; 218821.SAMN05421837_104565; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000198878; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046348; P:amino sugar catabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05007; SIS_Etherase; 1.
DR   Gene3D; 1.10.8.1080; -; 1.
DR   HAMAP; MF_00068; MurQ; 1.
DR   InterPro; IPR005488; Etherase_MurQ.
DR   InterPro; IPR005486; Glucokinase_regulatory_CS.
DR   InterPro; IPR040190; MURQ/GCKR.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   Pfam; PF13580; SIS_2; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00068};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00068}.
FT   DOMAIN          61..223
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   308 AA;  31676 MW;  CFCA7E2E2307EDE8 CRC64;
     MTVPTQAVHV DSPTETRNPR TTDIDLMSTA GILGAINAED RTVAGAVAAV LPQVARAVDY
     AVDALRAGGR VHYVGAGTSG RLATLDAAEL VPTFNVPSDW FIAHHAGGER ALRQAVENAE
     DDDGAGAAEM AAMVQPGDFV LGLTASGRTP YVLGALLAAS RQGARTGLVS GNPKAAKPAG
     VDVLIAVDTG PEAIAGSTRM KAGTAQKMIL TSFSTATMIK LGRTYSNLMV SMRATNAKLR
     GRTIRILQEA TGMTMADCSD ALTEAGGDLK VALVHLLSGE DVKSAAKALH ASGGHVRKAL
     DLVRVRAS
//
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