ID H1Y3U0_9SPHI Unreviewed; 678 AA.
AC H1Y3U0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000256|ARBA:ARBA00018546};
DE EC=3.5.1.52 {ECO:0000256|ARBA:ARBA00012158};
DE AltName: Full=Peptide:N-glycanase {ECO:0000256|ARBA:ARBA00032901};
GN ORFNames=Mucpa_6296 {ECO:0000313|EMBL:EHQ30352.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ30352.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ30352.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ30352.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001650};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CM001403; EHQ30352.1; -; Genomic_DNA.
DR RefSeq; WP_008512012.1; NZ_CM001403.1.
DR AlphaFoldDB; H1Y3U0; -.
DR STRING; 714943.Mucpa_6296; -.
DR eggNOG; COG1305; Bacteria.
DR HOGENOM; CLU_014876_0_0_10; -.
DR OrthoDB; 679512at2; -.
DR Proteomes; UP000002774; Chromosome.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR35532:SF5; CARB-BD_DOM_FAM9 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35532; SIMILAR TO POLYHYDROXYALKANOATE DEPOLYMERASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..678
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003558160"
FT DOMAIN 212..288
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|Pfam:PF01841"
FT DOMAIN 561..631
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
SQ SEQUENCE 678 AA; 77086 MW; DFBB4928AF6EA890 CRC64;
MFKINLFNKN NILIKAGIRL LLLIICQHSF SAFSQRPALT MQQKVTIAMN FAGENKAELQ
KVLDHYGASA RDSLKLRAAY FLIANMTGHF SYTGYQRQGV DSLIRYIVKA KQVAGNDFWQ
PGTFIQLDRL WFNVMAYASA KHSGPENTFD NKAISANLLI ENIEYAFKAW SLPWSRHLSF
DQFCTYVLPY RFYDEPLESW RPRYMEKFGW LAKAMGKSTD PVLACKLINE SLQREIPFNR
GLERYNKALS PSDLLLAGQA NCLNQAAAAN FAMRAMGIPV ALEVVRQWAN RSFGHKFSSV
IDKEGNFISI IGEEFLPHQT RLPYIAPKIF HLGYTIQDDS LMKARMSSGG LVADFDCFQT
DATRQLIPVK DLMVTIRPGT VKPGETVYLC VFDNRDWAPV CASASPDGKS VLFKDMGLGV
LYLPMVLRDK LMPVSSPLIL QNDQSIKPVI VNKGANDTIT LTRKYPLSQA KLDWLWLMLD
GKFEGADNPD FSGAKPLYTV QNPFAMMLNR RRIPRSNFRY VRYCFPKNAY GSLAEICFYG
DSLLKQPLKG QLIHSSKVHD SDVQKAFDGV LGNYIQTPDS SDYNGEWIGL DLGEPKAITG
VGFSPRNDEN GIDQYMSYEL YYWDDQWISL GPGTRVEDQI SKLKFSKVPK GALLWLRNHT
VGNEERIFLY ENHAQKWW
//
