AMPD_HAEIN
ID AMPD_HAEIN Reviewed; 184 AA.
AC P44624;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000250|UniProtKB:P13016};
DE EC=3.5.1.28 {ECO:0000250|UniProtKB:P13016};
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000250|UniProtKB:P13016};
GN Name=ampD; OrderedLocusNames=HI_0300;
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).
CC -!- FUNCTION: Involved in cell wall peptidoglycan recycling. Specifically
CC cleaves the amide bond between the lactyl group of N-acetylmuramic acid
CC and the alpha-amino group of the L-alanine in degradation products
CC containing an anhydro N-acetylmuramyl moiety.
CC {ECO:0000250|UniProtKB:P13016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000250|UniProtKB:P13016};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P82974};
CC Note=Zn(2+) is required for amidase activity.
CC {ECO:0000250|UniProtKB:P82974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13016}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21965.1; -; Genomic_DNA.
DR PIR; F64060; F64060.
DR RefSeq; NP_438467.1; NC_000907.1.
DR RefSeq; WP_005694366.1; NC_000907.1.
DR AlphaFoldDB; P44624; -.
DR SMR; P44624; -.
DR STRING; 71421.HI_0300; -.
DR EnsemblBacteria; AAC21965; AAC21965; HI_0300.
DR KEGG; hin:HI_0300; -.
DR PATRIC; fig|71421.8.peg.317; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_049290_1_0_6; -.
DR OMA; PFTDAQY; -.
DR PhylomeDB; P44624; -.
DR BioCyc; HINF71421:G1GJ1-318-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..184
FT /note="1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD"
FT /id="PRO_0000164414"
FT DOMAIN 30..171
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT ACT_SITE 120
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P75820"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82974"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82974"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82974"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P75820"
SQ SEQUENCE 184 AA; 21448 MW; B7A035527E328401 CRC64;
MRKIKDIEKG LLTDCRQIQS PHFDKRPNPQ DISLLVIHYI SLPPEQFGGG YVDDFFQGKL
DPKIHPYFAE IYQMRVSAHC LIERNGRITQ YVNFNDRAWH AGVSNFQGRE KCNDFAIGIE
LEGSNEQPFT DAQYFSLQEL TNVIMKSYPK ITKDRIVGHC DISPKRKIDP GQYFDWERYL
SSVK
