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Database: UniProt
Entry: D1BFR2_SANKS
LinkDB: D1BFR2_SANKS
Original site: D1BFR2_SANKS 
ID   D1BFR2_SANKS            Unreviewed;       916 AA.
AC   D1BFR2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=Sked_14870 {ECO:0000313|EMBL:ACZ21423.1};
OS   Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ21423.1, ECO:0000313|Proteomes:UP000000322};
RN   [1] {ECO:0000313|EMBL:ACZ21423.1, ECO:0000313|Proteomes:UP000000322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC   {ECO:0000313|Proteomes:UP000000322};
RX   PubMed=21304646;
RA   Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA   Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA   Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL   Stand. Genomic Sci. 1:110-118(2009).
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; CP001819; ACZ21423.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1BFR2; -.
DR   STRING; 446469.Sked_14870; -.
DR   CAZy; CBM61; Carbohydrate-Binding Module Family 61.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   KEGG; ske:Sked_14870; -.
DR   eggNOG; COG3867; Bacteria.
DR   HOGENOM; CLU_011259_1_1_11; -.
DR   Proteomes; UP000000322; 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:0015926; F:glucosidase activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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   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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361192};
KW   Hydrolase {ECO:0000256|RuleBase:RU361192};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|RuleBase:RU361192};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|RuleBase:RU361192"
FT   CHAIN           34..916
FT                   /note="Arabinogalactan endo-beta-1,4-galactanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361192"
FT                   /id="PRO_5005126070"
FT   TRANSMEM        885..905
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          438..492
FT                   /note="Bacterial Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF07532"
FT   REGION          721..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..751
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   916 AA;  95381 MW;  DF8A0843E1221C60 CRC64;
     MHPPRRRLPL RLAAAATAGA VLLTPLVTTS AVAADDPTGP VEAGIVVDKV EGLPEDFING
     VDISSILALE KSGVTFQDWD GQQADIFEVL ADADVNYVRV RVWNDPYDAQ GNGYGGGDND
     IAAAVAIGER ATAHGMRLLV DFHYSDFWAD PAKQQAPKAW AEMTVDQKAD ATEAYTADAL
     TQLRDANVDV GMVQVGNETN NSVAGVTGWA GMSQIFSAGS SAVRTVYPDA LVAVHFTNPE
     RAGSYANIAR QLDTHGVDYD VFASSYYPFW HGSLSNLTTV LDQVATTYDK QVMVAETSWN
     YTLEDGDGHE NTIKPTSGFT QYPSSVQGQA TAVRDVMQAV TDVGPEGIGV FYWEPAWLPV
     GPPEELAQNK LLWEEHGSGW ASSYAAEYDP EDAGEWYGGS SWDNQALFDF QGAPLESLRV
     FQYARTGATA PREVVDVEKV TLTVPDGSPV TLPATVRVTY NDGSTEDRPV TWSTSVDWIR
     GPGAYTVSGT TADGARVTAT VTVSAVNHVA NPSFEDATAA PWTITGTGAS VAADADASDG
     ARSLKFWSAT PYTFAVEQTI TGVPAGTYRL SATSQGALAG PTDTRTLSAT TAEGEQSAPI
     TLDGWRAFST ATVDDVVVGE DGLVTVAARY SLSGAAWGNL DDVRLTRVES TTTVDTAALE
     QSLQTARTVD RTLWTPASLA TLDVAVESAE VLLSGSRATQ EDVDAVTALV DAAVAGLEAI
     DTTPPVDPEP PVTPQPPVTP EPPVTPEPPV TPEPVTPVMT LSSGSVTAGD DVTVTVTGLD
     LPEVEIGIES EYQRLASATV VDGAATVTVT VPATLEAGTH SLQARDADGA VLAQAAVEVL
     AAPVATPTPG EPGTDAPTTP APGVPSSGAP AAGGTGTLSE TGADVALLAG LTTMLVAAGS
     AVLVLRRRRA GTSTLR
//
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