ID A0A1V3MZN6_9SPHI Unreviewed; 665 AA.
AC A0A1V3MZN6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BWD42_12920 {ECO:0000313|EMBL:OOG18163.1};
OS Sphingobacterium sp. CZ-UAM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG18163.1, ECO:0000313|Proteomes:UP000188865};
RN [1] {ECO:0000313|EMBL:OOG18163.1, ECO:0000313|Proteomes:UP000188865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG18163.1,
RC ECO:0000313|Proteomes:UP000188865};
RA Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA Zuniga C., Morales M., Revah S., Utrilla J.;
RT "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT methanotrophic consortium.";
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOG18163.1}.
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DR EMBL; MTCM01000002; OOG18163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3MZN6; -.
DR STRING; 1933868.BWD42_12920; -.
DR OrthoDB; 679512at2; -.
DR Proteomes; UP000188865; Unassembled WGS sequence.
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; 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; 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}.
FT DOMAIN 204..269
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|Pfam:PF01841"
SQ SEQUENCE 665 AA; 75473 MW; 62EFBFBE52BFC56F CRC64;
MKATLLTIFF LLSLSGLISY GQQRTVPEQQ LLSLSLDFAG KNKSNLQQVL DHYSKAPGDS
LKLRAARFLI ANMTGHFSYA GYLQKGMSDL IDHVKHLEDS LDRKMWRFYA DPLVDRAWDS
VINKSKAVNP SPSQVFDNKV INAQLLIENI DHAFEAWNYP WSKHLTFDEF CDYILPYRFY
DEPLESWRPL YREKFSWLVQ AMEKIGSTDP VDACRLINDS LRYKFTFNPA MFSYPAALGP
LEVLKGGMGK CLDQAGFANY AMRAMGIPVI LEQIPHWADR SMGHEFCSVR KKDGSFASFL
GAELPPGKNE IRNVAPKIYR TFYRIQDDRY LVDEVSLGDV SALFDRYQLD VTKEHIPVRD
IVLKLPDHSC VPGETIYICV FDNEKWIPFS STETADGKNA VFKDIGLGAV YLPMAIKSQM
LPLSAPLLLK KDGGLSEIRP TGSEVEKVVL SRKYPLGEKQ RAWLELVRGG LFQGAGSADF
SDAQEIIKIS WSEMAMNKYY YGNNGSFRYI RYVFPDSSFG SLAELAVYAD SLFQIPLKGK
PVASAKVKPE DVKIAFDGRL DNFIYTEAAD TYKGEWIGLD LGERTKITAV GLSPRNDTNG
IMQGMNYELF YWKDKWVSLG AGTLDSQLRL NYGRVPKGAL LLLRNHTEGK EERIFTYENG
KQVWW
//
