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Database: UniProt
Entry: A0A1H9I1F8_9BACI
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ID   A0A1H9I1F8_9BACI        Unreviewed;       301 AA.
AC   A0A1H9I1F8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=SAMN05216362_12225 {ECO:0000313|EMBL:SEQ68397.1};
OS   Piscibacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX   NCBI_TaxID=571933 {ECO:0000313|EMBL:SEQ68397.1, ECO:0000313|Proteomes:UP000199427};
RN   [1] {ECO:0000313|EMBL:SEQ68397.1, ECO:0000313|Proteomes:UP000199427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21633 {ECO:0000313|EMBL:SEQ68397.1,
RC   ECO:0000313|Proteomes:UP000199427};
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; FOES01000022; SEQ68397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9I1F8; -.
DR   STRING; 571933.SAMN05216362_12225; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000199427; 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; IPR000408; Reg_chr_condens.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR   PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS50012; RCC1_3; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199427}.
FT   DOMAIN          57..220
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   301 AA;  33190 MW;  4AD1A0D53A463BED CRC64;
     MMERLTKLMT ETYNPKSKEL DQLTTDRILQ LMNEEDMLIP KAISKVLPEI EETVEVVYQS
     FINNGRLFYV GAGTSGRIGL LDAVECPPTF STSSEMIQAV IAGGSDAMMV AVEGAEDNED
     LAVRDLKERQ LSEDDVVIGI AASGRTPYVK GALKYAQMVG AKAVSLSSNE ESEISHYADI
     AIEVITGPEV LTGSTRLKAA TAHKMILNMI STASMVKCGK VYQNLMVDVN ATNYKLKERC
     KKIVREATQV SYDEAEKVLQ ETDYKVKPAI VMILANVDYE QANLLLEQSK GFVREAIRKS
     D
//
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