ID G7VTU4_PAETH Unreviewed; 1304 AA.
AC G7VTU4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000256|RuleBase:RU361192};
DE EC=3.2.1.89 {ECO:0000256|RuleBase:RU361192};
GN OrderedLocusNames=HPL003_06955 {ECO:0000313|EMBL:AET58154.1};
OS Paenibacillus terrae (strain HPL-003).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET58154.1, ECO:0000313|Proteomes:UP000005876};
RN [1] {ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA Shin S.H., Kim S., Kim J.Y.;
RT "Complete sequence of Paenibacillus terrae HPL-003.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPL-003;
RA Shin S.H., Kim S., Kim J.Y.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AET58154.1, ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|EMBL:AET58154.1,
RC ECO:0000313|Proteomes:UP000005876};
RX PubMed=22328761; DOI=10.1128/JB.06668-11;
RA Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT Bacterium Isolated from Soil Found in Forest Residue.";
RL J. Bacteriol. 194:1266-1266(2012).
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; CP003107; AET58154.1; -; Genomic_DNA.
DR STRING; 985665.HPL003_06955; -.
DR KEGG; pta:HPL003_06955; -.
DR eggNOG; COG1361; Bacteria.
DR eggNOG; COG3867; Bacteria.
DR HOGENOM; CLU_261213_0_0_9; -.
DR Proteomes; UP000005876; Chromosome.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; IPR001119; SLH_dom.
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 Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51272; SLH; 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..21
FT /evidence="ECO:0000256|RuleBase:RU361192"
FT CHAIN 22..1304
FT /note="Arabinogalactan endo-beta-1,4-galactanase"
FT /evidence="ECO:0000256|RuleBase:RU361192"
FT /id="PRO_5005132849"
FT DOMAIN 1086..1153
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1159..1216
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1217..1280
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 810..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1304 AA; 140671 MW; DDC32A8213323A69 CRC64;
MLLVVAIMFS SWPMRLTPAA AAESAGVSAV VNGGFETDFW SDQSWQVEAS DWKQVDIQHY
AYASDPFITP SEDTYAFKYW INDAAPTDQQ VTVSQKLPTL QPGSYELSVQ SMGGADAKAG
HVQVFAGTDQ SSEVATSGYN QWGSVTLKFV LTEQTSDLVI GARISGAAAA WGYLDRFILK
QVSTDTAHPV AADIFVKKVE GLKSDFIKGV DISSILSLEQ SGVRFYNEQG TEQDIFQTLK
ESGVNYVRVR VWNHPYDAKG NGYGGGNNDL AKAIEIGKRA TNNGLKLLVD FHYSDFWADP
GKQHVPKAWQ NLSFADKEQA VYDYTRDSLQ KLIDQGIDVG MVQVGNETNQ SFIGEKDWTK
ISALFNKGSQ AVRAVDPNIL VALHFTNPET PGRYASYAKA LSDNHVDYDV FASSYYPFWH
GSLSNLTAVL KQVADTYGKK VMVAETSYAY TAEDGDGHEN TAPRSSGQTL DYPISAQGQA
TSVRNVIEAV SNVGDAGIGV FYWEPAWLPV GPKADVEQSK QLWERYGSGW AASYAAEYDP
DDAGKWYGGS AVDNQALFDF TGHPLPSLKV FNYVNTGAVA TLQVDEVQAI TVTADAGEKI
SLPDSVTVTY NDGSTGTLAV EWDQAALEQA VSQGAGSYVI NGTAKGGYPA QAVLEIRRPN
LLVNGGFELS DRSMWKITYG GESAPHTDYQ NKASDAKSGQ YSLHFYSADA VNFRVEQAVY
GLKPGYYDLS MSIQGGDAKN AQMKLFAATG GKEEKVDTGV NGWVQWNQPV IRDIRVTDGK
LTVGASIQAD GGAWGSLDDF YLTFVRDAEA TNPGEGTTPT PEPAPAPTPT PAPGSTPTPA
PGKDSSGNSS TGSGGTSAGQ SENVTVSVDG GKNSSTKLSN VVIQRTTLSD GSKKDQVSYG
AAQAREALSS VKAEGRSSVR LVMPDSKDEV TELEFALPKD TAKTLADAGV GLEVYTNHAR
LILSPSTLAS MDGNRQFTLS PVKSEAAIQA VAERAKQNGL VQAAAGQGEV RIIGRPVMIE
TNLQGQSVEL VLPLPQQSLP NSAEERQAFL SNLAVYVEHS DGTRELVQPT LLWDGNQPAG
LRFSVNKFST FTVLHLNKQI ASIGGEQESE RSQPYMQGYP DGTFQPARRM TRSELAEILF
RLAVDRSEQP LVESSAPQIR ANYTDVAGQN WAAEAIDTVT TAGWMKGYSS STFAPGRPIT
RAEMATALAR WNNLSGAASG TFPDTTGHWA KDDIARVQQA GYMHGMPDGS FQPDQNLSRA
EAVTLFNRVW KREPESFADS SRWSDVPVGH WAFGDIAAAT TRIR
//
