GH101_RENSM
ID GH101_RENSM Reviewed; 1509 AA.
AC A9WNA0; A9WNA1; A9WNA2; A9WNA3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Putative endo-alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.97 {ECO:0000250|UniProtKB:Q8DR60};
DE Flags: Precursor;
GN OrderedLocusNames=RSal33209_1326, RSal33209_1327, RSal33209_1328,
GN RSal33209_1329;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
RN [2]
RP IDENTIFICATION, AND FAMILY ASSIGNMENT.
RX PubMed=20556855; DOI=10.1142/s0219720010004628;
RA Naumoff D.G.;
RT "GH101 family of glycoside hydrolases: subfamily structure and evolutionary
RT connections with other families.";
RL J. Bioinform. Comput. Biol. 8:437-451(2010).
CC -!- FUNCTION: Probably involved in the breakdown of mucin-type O-linked
CC glycans. Specifically removes the T-antigen disaccharide (Gal-beta-1,3-
CC GalNAc-alpha) from extracellular host glycoproteins.
CC {ECO:0000250|UniProtKB:Q8DR60}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] = beta-D-galactosyl-(1->3)-N-
CC acetyl-D-galactosamine + L-threonyl-[protein]; Xref=Rhea:RHEA:54540,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13923, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:137950, ChEBI:CHEBI:546807;
CC EC=3.2.1.97; Evidence={ECO:0000250|UniProtKB:Q8DR60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] = beta-D-galactosyl-(1->3)-N-
CC acetyl-D-galactosamine + L-seryl-[protein]; Xref=Rhea:RHEA:30983,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13922, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:137949, ChEBI:CHEBI:546807;
CC EC=3.2.1.97; Evidence={ECO:0000250|UniProtKB:Q8DR60};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- MISCELLANEOUS: The hydrolysis reaction proceeds with retention of the
CC anomeric configuration. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 101 family. A subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The sequence shown here is a temptative reconstruction from
CC the four submitted CDS; the exact positions of the frameshifts are
CC unsure. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABY23063.1; Type=Frameshift; Note=Produces separate ORFs.; Evidence={ECO:0000305};
CC Sequence=ABY23064.1; Type=Frameshift; Note=Produces separate ORFs.; Evidence={ECO:0000305};
CC Sequence=ABY23065.1; Type=Frameshift; Note=Produces separate ORFs.; Evidence={ECO:0000305};
CC Sequence=ABY23066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABY23066.1; Type=Frameshift; Note=Produces separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; CP000910; ABY23063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000910; ABY23064.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000910; ABY23065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000910; ABY23066.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A9WNA0; -.
DR SMR; A9WNA0; -.
DR STRING; 288705.RSal33209_1326; -.
DR CAZy; CBM51; Carbohydrate-Binding Module Family 51.
DR CAZy; GH101; Glycoside Hydrolase Family 101.
DR EnsemblBacteria; ABY23063; ABY23063; RSal33209_1326.
DR EnsemblBacteria; ABY23064; ABY23064; RSal33209_1327.
DR EnsemblBacteria; ABY23065; ABY23065; RSal33209_1328.
DR EnsemblBacteria; ABY23066; ABY23066; RSal33209_1329.
DR KEGG; rsa:RSal33209_1326; -.
DR KEGG; rsa:RSal33209_1327; -.
DR KEGG; rsa:RSal33209_1328; -.
DR KEGG; rsa:RSal33209_1329; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1470; Bacteria.
DR HOGENOM; CLU_406451_0_0_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050110; F:mucinaminylserine mucinaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd14244; GH_101_like; 1.
DR Gene3D; 2.60.120.1060; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR025706; Endoa_GalNAc.
DR InterPro; IPR040633; Gal_mutarotas_3.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040502; GalBD-like.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR035364; Glyco_hyd_101_beta.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR038637; NPCBM_sf.
DR Pfam; PF18080; Gal_mutarotas_3; 1.
DR Pfam; PF17974; GalBD_like; 1.
DR Pfam; PF17451; Glyco_hyd_101C; 1.
DR Pfam; PF12905; Glyco_hydro_101; 1.
DR Pfam; PF08305; NPCBM; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Calcium; Cell wall; Glycosidase; Hydrolase; Metal-binding;
KW Peptidoglycan-anchor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1478
FT /note="Putative endo-alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000408866"
FT PROPEP 1479..1509
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000408867"
FT REGION 313..585
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 1176..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1475..1479
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT ACT_SITE 472
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 498
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 878
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 880
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 926
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 929
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1478
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1509 AA; 157347 MW; 6700242A747EE1A5 CRC64;
MPFRGRRRQS ALRGLSLAAT FCLAAGSSGI SGALFATPAQ ADPLPTAAGL SINSANLTVE
VSADFPQALS YTETSSAKHL SGARTLASSI TINGTDQPVK VSSQKADAQT VNYLITPNNL
AGVSLDAQLR VEGMTLTFKI SKIKDTAENR VNNLQIKNQD LVTVSSQEPG ATVASAVVSV
DRAVSGDTIT NLSSTTALDP TAKRSMLAIA ATDQLAAGFE TNSLYDSGNT IGPSDQGKFW
RQALADGTGA DGKPAVKMAV SSGAWLYRSA GSDQTEELPW SKVVISGDAN ADGKVDWQDG
AIAYRSIESK PAGGDDVKNR VVTHIPFNFA SQATHPFLRT LDDVKHIALA TDGLGQMALE
KGYTSEGHDS ANSDFGGNFN ERAGGLTDFN AMLSGGSAYG ATFGVHINNT EAYPEANSFS
NDFVDPTKKG WNWLDQSFYI DQQRDILSGS QQQRIDQLRS EAGPNLTMAY VDVYYESGWK
SYRLQKGLKD AGFSVASEFA TAMPANNTWS HWANDEKHGG SNNIKAGTQI LRFVDNSQRD
IWNPDPLLGT SHIVEWEGWT NQNDYNAFLK NIWGNNLPVK FLQQQQITSW KSRSVDLTGG
LKVTGTSLAD RVISQQGVPV LKGSNYLLPW SAAPVSFGSG AVNDTTQNKL YHYSADGGTS
TWQLTPQFAT ASSLQIYKLT DYGRELIGSV PVVNGSVTLT AEANQAYVLV ADASVTTVPA
DPSYGAGSKV KDPGFNSAGL KDWNATGGAA VERTAQGLLV AKLGQGSSAI SQTLGSLDPG
SYSIGAWVEI EPTTLTVTPA GGAPISVTVD QSGAENFVAS DEKRGTYFQR LRVLVDIANA
GAPQLSISAP AGEAAVRIDD VRVVKANKVP TTGILSENFE NTDQGWLPFI KGDAGGQTDP
RTHIAKLNAP YTQKGWNGKT TSDVLDDTYS LHSHEENQGL VYRTSNYTLP LQAGRQYRVS
FDYQASLANQ YTWVSGYDSG KNPVQTASTA IPVATDTTRW SQTLSAGSCG PAWVGLQRTG
SSGGAEFSMD NLLVEDLGPS AETPACASLS LTSGQDVIEQ GQTNTFSASF SSSEAQSIAG
LSVALDLPAG WTASAATPAT AATLPAGGSL ETQWKVQVPA DADGDYTIKA KASYQTTVDP
IGSRSATTET AVYTLPKPPT KDTYASDMQW IGTPSNGWGP VEKDQANGEQ AQGDGPPLKL
GGVTYPKGLG AHAASSIRYY VGSQCSAFTA VIGIDDFQKL KGQAVFSVLG DGNSLYTSPV
MKGGAAAQTI TVPLNGAKYV DLKVAISGAN NGNAWSDWAN AKFLCSAPVA PITLQPTLSV
PTDSLQPGSA FTVRVDQLKS GSTAKAELHS DPIDLGSVQA NNDGVASFQV TLAQDAPLGN
HQIVVTGTDK NGLAATGTVD AQIKAANPNP GTGSNPGTGS NPGTDPGTGS AGGNSSGGGA
NGSGANGTYV NGSGGSFGNG AGMDAKTGSN SASSLAETGF SGLVLPLGIG LMLLLIGAAA
IIVRRHRHS
