ID G5ST98_9BACT Unreviewed; 645 AA.
AC G5ST98;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HMPREF9441_02599 {ECO:0000313|EMBL:EHG99471.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG99471.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG99471.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG99471.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-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}.
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:EHG99471.1}.
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DR EMBL; AFFY01000038; EHG99471.1; -; Genomic_DNA.
DR RefSeq; WP_008621223.1; NZ_JH376609.1.
DR AlphaFoldDB; G5ST98; -.
DR STRING; 762968.HMPREF9441_02599; -.
DR GeneID; 78583498; -.
DR PATRIC; fig|762968.3.peg.2317; -.
DR eggNOG; COG1305; Bacteria.
DR HOGENOM; CLU_014876_0_0_10; -.
DR OrthoDB; 679512at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 211..280
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|Pfam:PF01841"
SQ SEQUENCE 645 AA; 75574 MW; A7BE7AE547E642D3 CRC64;
MKNLLLCCLA ATLAVSSCQK TSIRQTLEKA GENRRELETV LEHYKNEPLK EKAARFLLEN
MDGHFAHTGE AVDVYDNYMD SVFRHCNGDR VFWIMKYDTI LQRTGLDLEL SQDERLYDAQ
SVTADFLTEH IDSAFTVWQQ NWNKQYSFEM FCRYVLPYRI GNEKTSLWRK TFTVPSWVRE
AYAPNQDNST YAYGMANDIL GGMRSVIYYP PQFLPDLPLT ALEHVKSASC KEYAHLCVAV
LRAHGLPATI DFTPQWGNRG LGHEWCVFFP DNHSFIPFNP GERLGDHFMK RKEDRLTKVF
RQTYEKQPES LYMQNKGEEE IPDLFDTPYI MDVTREYTAT SDVEVELYDD VESGRFVYLS
VFDNQDWSIV HWGTRHGRKA TFRDMARNVV YMPVHYSEEN GTVPAGDAFL LDPRGNIHKM
TADTTQRTTV EVKRKFRDVR SNQFLQGVIG GKFQVANQED FSDSLTIHVI PHLKDNKFHV
VHPRYIGEYR YFRYLSPDWS RGNMAELYTF NAAGDTLKHK RLMGNFHVRP WCGPENLFDG
NVLSFYDSHD VYGVWYGWEL EQPENVARIV FLPRNDDNFI REGEEYELFY WNHGTWMSLG
RKTGNFEAVL KYDNVPAQAL FRLHNRTKGS EERIFTYEDG KQIWW
//
