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   27-MAR-2024, entry version 123.
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; Pseudomonadota; 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   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   OrthoDB; 9794842at2; -.
DR   PhylomeDB; P44624; -.
DR   BioCyc; HINF71421:G1GJ1-318-MONOMER; -.
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; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417:SF4; 1,6-ANHYDRO-N-ACETYLMURAMYL-L-ALANINE AMIDASE AMPD; 1.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 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
//