PGRP2_HUMAN
ID PGRP2_HUMAN Reviewed; 576 AA.
AC Q96PD5; A8K050; A8K8C7; B2RMZ2; B7ZM33; Q68CK1; Q96N74; Q9UC60;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase;
DE EC=3.5.1.28;
DE AltName: Full=Peptidoglycan recognition protein 2;
DE AltName: Full=Peptidoglycan recognition protein long;
DE Short=PGRP-L;
DE Flags: Precursor;
GN Name=PGLYRP2; Synonyms=PGLYRPL, PGRPL; ORFNames=UNQ3103/PRO10102;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11461926; DOI=10.1074/jbc.m105566200;
RA Liu C., Xu Z., Gupta D., Dziarski R.;
RT "Peptidoglycan recognition proteins: a novel family of four human innate
RT immunity pattern recognition molecules.";
RL J. Biol. Chem. 276:34686-34694(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-394.
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-46;
RP GLN-99; LYS-270 AND GLN-394.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver, Mammary gland, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 22-36.
RX PubMed=7663175; DOI=10.1006/prep.1995.1049;
RA De Pauw P., Neyt C., Vanderwinkel E., Wattiez R., Falmagne P.;
RT "Characterization of human serum N-acetylmuramyl-L-alanine amidase purified
RT by affinity chromatography.";
RL Protein Expr. Purif. 6:371-378(1995).
RN [8]
RP PROTEIN SEQUENCE OF 22-36.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP SER-239, DEAMIDATION AT ASN-274 AND ASN-322, AND DISULFIDE BONDS.
RC TISSUE=Liver, and Serum;
RX PubMed=16054449; DOI=10.1016/j.bbapap.2005.07.001;
RA Zhang Y., van der Fits L., Voerman J.S., Melief M.-J., Laman J.D., Wang M.,
RA Wang H., Wang M., Li X., Walls C.D., Gupta D., Dziarski R.;
RT "Identification of serum N-acetylmuramoyl-l-alanine amidase as liver
RT peptidoglycan recognition protein 2.";
RL Biochim. Biophys. Acta 1752:34-46(2005).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF HIS-411;
RP CYS-419; HIS-436; TRP-442 AND CYS-530.
RX PubMed=14506276; DOI=10.1074/jbc.m307758200;
RA Wang Z.-M., Li X., Cocklin R.R., Wang M., Wang M., Fukase K., Inamura S.,
RA Kusumoto S., Gupta D., Dziarski R.;
RT "Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine
RT amidase.";
RL J. Biol. Chem. 278:49044-49052(2003).
RN [11]
RP GLYCOSYLATION AT ASN-485.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77; ASN-367 AND ASN-485.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367 AND ASN-485.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: May play a scavenger role by digesting biologically active
CC peptidoglycan (PGN) into biologically inactive fragments. Has no direct
CC bacteriolytic activity. {ECO:0000269|PubMed:14506276}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00806};
CC -!- INTERACTION:
CC Q96PD5-2; O43765: SGTA; NbExp=3; IntAct=EBI-12758027, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Secreted. Membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PD5-2; Sequence=VSP_008964;
CC -!- TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver, and
CC secreted into serum. Expressed to a much lesser extent in transverse
CC colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach
CC and testis. Isoform 2 is not detected in the liver or serum.
CC {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16054449}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AF384856; AAL05629.1; -; mRNA.
DR EMBL; AB073610; BAD38647.1; -; mRNA.
DR EMBL; AY358156; AAQ88523.1; -; mRNA.
DR EMBL; AK055882; BAB71034.1; -; mRNA.
DR EMBL; AK289415; BAF82104.1; -; mRNA.
DR EMBL; AK292292; BAF84981.1; -; mRNA.
DR EMBL; CH471106; EAW84482.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84483.1; -; Genomic_DNA.
DR EMBL; BC136551; AAI36552.1; -; mRNA.
DR EMBL; BC136552; AAI36553.1; -; mRNA.
DR EMBL; BC144238; AAI44239.1; -; mRNA.
DR CCDS; CCDS12330.2; -. [Q96PD5-1]
DR CCDS; CCDS86718.1; -. [Q96PD5-2]
DR RefSeq; NP_443122.3; NM_052890.3. [Q96PD5-1]
DR RefSeq; XP_006722696.1; XM_006722633.3.
DR AlphaFoldDB; Q96PD5; -.
DR SMR; Q96PD5; -.
DR BioGRID; 125340; 2.
DR IntAct; Q96PD5; 3.
DR STRING; 9606.ENSP00000345968; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 784; 8 N-Linked glycans (3 sites), 1 O-Linked glycan (1 site).
DR GlyGen; Q96PD5; 10 sites, 12 N-linked glycans (3 sites), 4 O-linked glycans (7 sites).
DR iPTMnet; Q96PD5; -.
DR PhosphoSitePlus; Q96PD5; -.
DR BioMuta; PGLYRP2; -.
DR DMDM; 38258222; -.
DR jPOST; Q96PD5; -.
DR MassIVE; Q96PD5; -.
DR PaxDb; Q96PD5; -.
DR PeptideAtlas; Q96PD5; -.
DR PRIDE; Q96PD5; -.
DR ProteomicsDB; 77669; -. [Q96PD5-1]
DR ProteomicsDB; 77670; -. [Q96PD5-2]
DR Antibodypedia; 43600; 99 antibodies from 22 providers.
DR DNASU; 114770; -.
DR Ensembl; ENST00000292609.8; ENSP00000292609.3; ENSG00000161031.13. [Q96PD5-2]
DR Ensembl; ENST00000340880.5; ENSP00000345968.4; ENSG00000161031.13. [Q96PD5-1]
DR GeneID; 114770; -.
DR KEGG; hsa:114770; -.
DR MANE-Select; ENST00000340880.5; ENSP00000345968.4; NM_052890.4; NP_443122.3.
DR UCSC; uc002nbf.5; human. [Q96PD5-1]
DR CTD; 114770; -.
DR DisGeNET; 114770; -.
DR GeneCards; PGLYRP2; -.
DR HGNC; HGNC:30013; PGLYRP2.
DR HPA; ENSG00000161031; Tissue enriched (liver).
DR MIM; 608199; gene.
DR neXtProt; NX_Q96PD5; -.
DR OpenTargets; ENSG00000161031; -.
DR PharmGKB; PA134929965; -.
DR VEuPathDB; HostDB:ENSG00000161031; -.
DR eggNOG; ENOG502QR3D; Eukaryota.
DR GeneTree; ENSGT00940000158718; -.
DR HOGENOM; CLU_038892_0_0_1; -.
DR InParanoid; Q96PD5; -.
DR OMA; RCAADMR; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q96PD5; -.
DR TreeFam; TF323898; -.
DR BRENDA; 3.5.1.28; 2681.
DR PathwayCommons; Q96PD5; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; Q96PD5; -.
DR BioGRID-ORCS; 114770; 12 hits in 1065 CRISPR screens.
DR ChiTaRS; PGLYRP2; human.
DR GeneWiki; PGLYRP2; -.
DR GenomeRNAi; 114770; -.
DR Pharos; Q96PD5; Tbio.
DR PRO; PR:Q96PD5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96PD5; protein.
DR Bgee; ENSG00000161031; Expressed in right lobe of liver and 42 other tissues.
DR ExpressionAtlas; Q96PD5; baseline and differential.
DR Genevisible; Q96PD5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:CACAO.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR GO; GO:0016019; F:peptidoglycan immune receptor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051701; P:biological process involved in interaction with host; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; IEA:Ensembl.
DR GO; GO:0001519; P:peptide amidation; NAS:UniProtKB.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:7663175"
FT CHAIN 22..576
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /id="PRO_0000023920"
FT DOMAIN 406..532
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT REGION 550..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT SITE 447
FT /note="Important for catalytic activity; essential for
FT amidase activity and zinc hydrate coordination"
FT /evidence="ECO:0000250|UniProtKB:P00806"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16054449"
FT MOD_RES 274
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:16054449"
FT MOD_RES 322
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:16054449"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT DISULFID 419..425
FT /evidence="ECO:0000269|PubMed:16054449"
FT VAR_SEQ 548..576
FT /note="TVKPRPARSVSKRSRREPPPRTLPATDLQ -> VSLRSLHYTARRPSVYTSS
FT TRPLPPACNSCARTASARPPTSRRHVYSGNLGPAFAGHSAGNIPDPVTSAYAASAQPQT
FT QPACPFPSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008964"
FT VARIANT 46
FT /note="T -> A (in dbSNP:rs3813135)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_050498"
FT VARIANT 99
FT /note="R -> Q (in dbSNP:rs733731)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_050499"
FT VARIANT 257
FT /note="T -> N (in dbSNP:rs28404490)"
FT /id="VAR_050500"
FT VARIANT 270
FT /note="M -> K (in dbSNP:rs892145)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_050501"
FT VARIANT 394
FT /note="R -> Q (in dbSNP:rs34440547)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15221005"
FT /id="VAR_055231"
FT VARIANT 476
FT /note="R -> W (in dbSNP:rs2304200)"
FT /id="VAR_050502"
FT MUTAGEN 411
FT /note="H->A: No effect on amidase activity."
FT /evidence="ECO:0000269|PubMed:14506276"
FT MUTAGEN 419
FT /note="C->A: Abolishes amidase activity."
FT /evidence="ECO:0000269|PubMed:14506276"
FT MUTAGEN 436
FT /note="H->A: No effect on amidase activity."
FT /evidence="ECO:0000269|PubMed:14506276"
FT MUTAGEN 442
FT /note="W->A: Reduced amidase activity."
FT /evidence="ECO:0000269|PubMed:14506276"
FT MUTAGEN 447
FT /note="Y->A: Abolishes amidase activity."
FT MUTAGEN 530
FT /note="C->S: Abolishes amidase activity."
FT /evidence="ECO:0000269|PubMed:14506276"
FT CONFLICT 124
FT /note="L -> P (in Ref. 6; AAI44239)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> G (in Ref. 4; BAB71034)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="R -> G (in Ref. 4; BAF82104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 62217 MW; 73EA8713DC54F85A CRC64;
MAQGVLWILL GLLLWSDPGT ASLPLLMDSV IQALAELEQK VPAAKTRHTA SAWLMSAPNS
GPHNRLYHFL LGAWSLNATE LDPCPLSPEL LGLTKEVARH DVREGKEYGV VLAPDGSTVA
VEPLLAGLEA GLQGRRVINL PLDSMAAPWE TGDTFPDVVA IAPDVRATSS PGLRDGSPDV
TTADIGANTP DATKGCPDVQ ASLPDAKAKS PPTMVDSLLA VTLAGNLGLT FLRGSQTQSH
PDLGTEGCWD QLSAPRTFTL LDPKASLLTM AFLNGALDGV ILGDYLSRTP EPRPSLSHLL
SQYYGAGVAR DPGFRSNFRR QNGAALTSAS ILAQQVWGTL VLLQRLEPVH LQLQCMSQEQ
LAQVAANATK EFTEAFLGCP AIHPRCRWGA APYRGRPKLL QLPLGFLYVH HTYVPAPPCT
DFTRCAANMR SMQRYHQDTQ GWGDIGYSFV VGSDGYVYEG RGWHWVGAHT LGHNSRGFGV
AIVGNYTAAL PTEAALRTVR DTLPSCAVRA GLLRPDYALL GHRQLVRTDC PGDALFDLLR
TWPHFTATVK PRPARSVSKR SRREPPPRTL PATDLQ
