ID A0A229VVS0_9BIFI Unreviewed; 1845 AA.
AC A0A229VVS0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000256|RuleBase:RU361192};
DE EC=3.2.1.89 {ECO:0000256|RuleBase:RU361192};
GN ORFNames=Tam10B_2036 {ECO:0000313|EMBL:OXM99718.1};
OS Bifidobacterium vansinderenii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1984871 {ECO:0000313|EMBL:OXM99718.1, ECO:0000313|Proteomes:UP000215433};
RN [1] {ECO:0000313|EMBL:OXM99718.1, ECO:0000313|Proteomes:UP000215433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tam10B {ECO:0000313|EMBL:OXM99718.1,
RC ECO:0000313|Proteomes:UP000215433};
RA Lugli G.A., Duranti S., Mangifesta M.;
RT "Bifidobacterium vansinderenii sp. nov.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic
CC linkages in type I arabinogalactans.; EC=3.2.1.89;
CC Evidence={ECO:0000256|RuleBase:RU361192};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family.
CC {ECO:0000256|ARBA:ARBA00010687, ECO:0000256|RuleBase:RU361192}.
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:OXM99718.1}.
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DR EMBL; NEWD01000031; OXM99718.1; -; Genomic_DNA.
DR Proteomes; UP000215433; Unassembled WGS sequence.
DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 2.60.40.3630; -; 1.
DR Gene3D; 2.80.10.50; -; 7.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.4270; Listeria-Bacteroides repeat domain; 3.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR011683; Glyco_hydro_53.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR022038; Ig-like_bact.
DR InterPro; IPR013378; InlB-like_B-rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR NCBIfam; TIGR02543; List_Bact_rpt; 2.
DR PANTHER; PTHR34983; ARABINOGALACTAN ENDO-BETA-1,4-GALACTANASE A; 1.
DR PANTHER; PTHR34983:SF2; ENDO-BETA-1,4-GALACTANASE; 1.
DR Pfam; PF07523; Big_3; 1.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF09479; Flg_new; 3.
DR Pfam; PF07745; Glyco_hydro_53; 2.
DR Pfam; PF14200; RicinB_lectin_2; 3.
DR SMART; SM00458; RICIN; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF50370; Ricin B-like lectins; 3.
DR PROSITE; PS50231; RICIN_B_LECTIN; 3.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361192};
KW Hydrolase {ECO:0000256|RuleBase:RU361192};
KW Signal {ECO:0000256|RuleBase:RU361192}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU361192"
FT CHAIN 28..1845
FT /note="Arabinogalactan endo-beta-1,4-galactanase"
FT /evidence="ECO:0000256|RuleBase:RU361192"
FT /id="PRO_5011828827"
FT DOMAIN 1380..1522
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 1544..1682
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 1704..1843
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 56..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1845 AA; 197671 MW; B56CCC54E5EDBEC6 CRC64;
MSRKPLAAVC AAVAALSMLV PASMASAADA SGTASNATAN VGQDYASSSA AKRAEAAKNA
AAAQQQLLEE SSQTPASASP TAENPNYPKE WNEGTDTGVT KLPASVTGVS SMTADTVRGV
NLTSYQAEKT AGVKFHDFNG NEIDDAGLMQ LLKSSGVNYV LLKVAVNPAD AKGNTYGGGN
PTLDNALKTA KVAQANGLKV NIQFLYSDFY TSKTVQKLPK GWPTSKDDLK TKVADYTKQS
LATLKSGGVT PDMVTIGSEI SSPYYDDNKA LQGGFLGMDN WEAIAALIEE ASKAVSANSK
NTTIAVGVSS VTPVLVTTYV DMLKYYEVDY DVLGTKVYAA YDDLAALAQT RKMVSEEYGK
SMAVLDTLYP FTQYDSDGQS NTTGGDDLIA AGKTLSPQAQ ADYMRSLYKS IVSAKNNANG
AGVFYGDATW IAVKAGLWHA DANWNAANEF GTGWVSKYAA DYVDYANNGG ASQQDDAALF
DDLGQPLQSL KMFAQLAAAN PSDADLVPAA QDPYADGSDT GASKETASVK SIPTVTNDTI
RGADVSSYQT LYAAGVRFKN FEGKEEPLFK ILKDNGMNWV RLRLFNDPKD SQNRYYGGGN
NDLKNVTEMA KEATKYGLKV NVDIHYNDFY SSSWRTPKAW KNHDYNQLKT DVADYTAEFM
KAMKDNNVDL GMVQIGNESN CGLLGVTVCS NGYSFDKDPN WGRLVELMNS AAKVIRKESP
STQIAVHMMY SDSWTINVIA DNFQKYGLDY DVFGMTYYPF WSAGSDNTDS HDGMAALIKS
EKVITETYKK KFAVMEFSQP FTTSDSDGFA NNLTDGGVSD YAASAQGQAD VIHDIMKTVT
ETDNGTDLGL GAFYWEPAWI AVVPGTNHWQ INRTYSNDYG TGWASEYSKD NDPNNTEYDS
WGASGWDNQA LFDDHGNALQ SLKAFTQIIA DRTVSFDTQG GDAMQSVTVK DGSTISKPAD
PVRAGYSFTG WTSDKEGKNA VDFSKPVTGD TTLYAQWGTN SYTVRFHAND GSNPEKTNDQ
KLAYGKDAEL TKNTFTRDGW TFNGWNTKAD GTGDSFDDGQ KVSNLTDQAN GVFDLYAKWT
PGVTGLAITA NPTKTSYHVG DTFDATGLAV AAKLADGSQR ALDPSEYTVS SPDMSTVGTK
TVTVTYAPAG SQNGKQTATF DITVEPGDRN SLQNSLNAAD KLNENDYTAD SWKALADARE
NARKVLADQN ATDKQIQDAA AMLGEATSKL VRAYTVRFDS RGGSSTAEQK VAEGKKAEKP
ADPTRSGYTF TGWTTDAEGR DAYDFNTAVT ADVQLYAQWK NIVAVAAPDA VSTPARKAPT
LPKTVEVTWS DGKTAKADVK WDAVAKSQYA QVGPFDVRGT IDGWDQGVTV HVNVTIGTGT
YAIATALNGG ERVFDIPGGS TAARANVQLY DRNGTAAQKY RVTALKNGNY TIVNQGSRLP
LAYSLRAGNG SRIQQREGSD TYGTEWRIDL TDDGSFTIRP AANGLENMAL DVPGANNSNG
SLLQLWSFTQ DGVNLAQRWK FLDATSPREK LDRLADDHRD DLKNGTYTVS SALKDSAVLD
VTGGSTGNGA NVQLYGSNGT DAQIWKVTHD DDGYVTLKNA NSGKVLDVSG GSANNGANVQ
QYDSNGTYAQ KWVAVKSGSA FKLVSALSPN LVIDVSGGSS ANGANVQIWD SNDTKAQRWS
FSAAKTLRTR IDELAAEHKS DVAEGTYEIA STAKDSMRFD VVGASRDDGA NVQLYGANGT
NAQRWKVSID AKGYATLTNV ASGKVLDISG ASTAEGANVQ QYGSNGSWAQ KWILKKNANG
SITLISALRE NFVIDAAGGG TTNGTNIQMW SSNGSAAQRW TFVKK
//
