ID A0A387B8Z8_9MICO Unreviewed; 860 AA.
AC A0A387B8Z8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=D7I47_04865 {ECO:0000313|EMBL:AYF97655.1};
OS Protaetiibacter intestinalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Protaetiibacter.
OX NCBI_TaxID=2419774 {ECO:0000313|EMBL:AYF97655.1, ECO:0000313|Proteomes:UP000278886};
RN [1] {ECO:0000313|Proteomes:UP000278886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFWR-13 {ECO:0000313|Proteomes:UP000278886};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFWR-13.";
RL Submitted (SEP-2018) 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}.
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DR EMBL; CP032630; AYF97655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387B8Z8; -.
DR KEGG; lyd:D7I47_04865; -.
DR OrthoDB; 3981930at2; -.
DR Proteomes; UP000278886; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR011683; Glyco_hydro_53.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR PANTHER; PTHR34983; ARABINOGALACTAN ENDO-BETA-1,4-GALACTANASE A; 1.
DR PANTHER; PTHR34983:SF2; ENDO-BETA-1,4-GALACTANASE; 1.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF07745; Glyco_hydro_53; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361192};
KW Hydrolase {ECO:0000256|RuleBase:RU361192};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000278886};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 835..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 820..834
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REGION 717..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 89666 MW; 4FE2E840CDB1DC98 CRC64;
MHAHSIRTGL GIGAVTAVAL ALVGIPSAIA AADGPVEAGI FVDRIDGLGD DFINGVDVSS
ILSEEESGVV YYDTEGHQAD LFDVLEDADI NYVRVRVWDD PYDAEGNGYG GGTTDLARAV
EIGERATAHG MRVLVDFHYS DFWADPAKQH VPKAWEGYTT EQLVTALGAY TEASLDAFAD
AGVDVGMVQI GNETNNTIAG VADWDGKAAM FSAGSAAVRE VFPDALVALH FTNPETPNRY
TGYAAQLAAH DVDYDVFASS YYNFWHGSPE NLTSVLSTIA DSYDKKVMVA ETSYVYTFDD
GDGWQNSVNA GNFSGDYPAT VQGQADLIHD VMAAVAAVGD AGLGVFYWEP AWIPVGTPDQ
LAANQQKWEQ YGSGWASSYA GSYDPVDAGV YYGGSSWDNQ ALFDFTGHPL ESLQTFRYAR
TGAVTERVAT SIETVALTVY DGSPIALPAT IEVGYNDGST EHPAVAWSDA VDWIRGPGVY
SIPGTIASGE AITATVTVLQ ANYVVNHGFE DADTSMWSLA TNPSGAASIT TTSNTNEGTK
ALDFWAASAF TIQLQQTVTG VPAGEYTLQA TAQGGALGDS DTLTLWAYTD DDSADTWMWL
YGWRDYRTFT TPPLTVGDDG TVTVGAYISA TGGAWGTLDD LRLVRYIPDA ALDTGALEEL
LDEADGVDRA LYTEGSLGGL DDAVASAQVV LAGSGDQDDV DAVVALLRAA LDGLALAPSG
EPSGEPSGEP SEGPVDAPVI TLGAGTVTPG GTLHVTVSGL EEGSIEIGVA STYRALATAS
VVAGTASATV TIPADLEAGL HHIQVRDGSG ALLAEAELRV LALGDTGADE TVIRVLAALG
AVLVLGGAAA FAWGRRRAAA
//