MURQ_HAEIN
ID MURQ_HAEIN Reviewed; 303 AA.
AC P44862;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase;
DE Short=MurNAc-6-P etherase;
DE EC=4.2.1.126;
DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase;
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase;
GN Name=murQ; OrderedLocusNames=HI_0754;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of hypothetical protein HI0754 from Haemophilus
RT influenzae.";
RL Submitted (JAN-2005) to the PDB data bank.
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. Together with AnmK, is also required for the utilization of
CC anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the
CC medium or derived from its own cell wall murein, and thus plays a role
CC in cell wall recycling (By similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC22413.1; -; Genomic_DNA.
DR PIR; I64090; I64090.
DR RefSeq; NP_438913.1; NC_000907.1.
DR RefSeq; WP_005693153.1; NC_000907.1.
DR PDB; 1NRI; X-ray; 1.90 A; A=1-303.
DR PDB; 4LZJ; X-ray; 2.40 A; A/B/C/D=1-303.
DR PDB; 4M0D; X-ray; 2.58 A; A/B/C/D=1-303.
DR PDBsum; 1NRI; -.
DR PDBsum; 4LZJ; -.
DR PDBsum; 4M0D; -.
DR AlphaFoldDB; P44862; -.
DR SMR; P44862; -.
DR STRING; 71421.HI_0754; -.
DR EnsemblBacteria; AAC22413; AAC22413; HI_0754.
DR KEGG; hin:HI_0754; -.
DR PATRIC; fig|71421.8.peg.792; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_6; -.
DR OMA; TRNPATM; -.
DR PhylomeDB; P44862; -.
DR BioCyc; HINF71421:G1GJ1-792-MON; -.
DR BRENDA; 4.2.1.126; 2529.
DR UniPathway; UPA00342; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; P44862; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IBA:GO_Central.
DR GO; GO:0016803; F:ether hydrolase activity; IBA:GO_Central.
DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046348; P:amino sugar catabolic process; IBA:GO_Central.
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 GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR CDD; cd05007; SIS_Etherase; 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 PANTHER; PTHR10088; PTHR10088; 1.
DR PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00274; TIGR00274; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Lyase; Reference proteome.
FT CHAIN 1..303
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000214836"
FT DOMAIN 61..224
FT /note="SIS"
FT ACT_SITE 89
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /evidence="ECO:0000250"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:4LZJ"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 42..66
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1NRI"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 202..221
FT /evidence="ECO:0007829|PDB:1NRI"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4LZJ"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:1NRI"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:4LZJ"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:4LZJ"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:4LZJ"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:4LZJ"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4LZJ"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:4LZJ"
SQ SEQUENCE 303 AA; 32532 MW; 789297C871248BD6 CRC64;
MNDIILKSLS TLITEQRNPN SVDIDRQSTL EIVRLMNEED KLVPLAIESC LPQISLAVEQ
IVQAFQQGGR LIYIGAGTSG RLGVLDASEC PPTFGVSTEM VKGIIAGGEC AIRHPVEGAE
DNTKAVLNDL QSIHFSKNDV LVGIAASGRT PYVIAGLQYA KSLGALTISI ASNPKSEMAE
IADIAIETIV GPEILTGSSR LKSGTAQKMV LNMLTTASMI LLGKCYENLM VDVQASNEKL
KARAVRIVMQ ATDCNKTLAE QTLLEADQNA KLAIMMILST LSKSEAKVLL ERHQGKLRNA
LSK
