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Database: UniProt/TrEMBL
Entry: A0A075V356_9PSEU
LinkDB: A0A075V356_9PSEU
Original site: A0A075V356_9PSEU 
ID   A0A075V356_9PSEU        Unreviewed;       840 AA.
AC   A0A075V356;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:AIG77225.1};
GN   ORFNames=AJAP_21835 {ECO:0000313|EMBL:AIG77225.1};
OS   Amycolatopsis japonica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX   NCBI_TaxID=208439 {ECO:0000313|EMBL:AIG77225.1, ECO:0000313|Proteomes:UP000028492};
RN   [1] {ECO:0000313|EMBL:AIG77225.1, ECO:0000313|Proteomes:UP000028492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG417-CF17 (DSM 44213) {ECO:0000313|Proteomes:UP000028492};
RX   PubMed=25193710; DOI=10.1016/j.jbiotec.2014.08.034;
RA   Stegmann E., Albersmeier A., Spohn M., Gert H., Weber T., Wohlleben W.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Amycolatopsis japonica
RT   MG417-CF17(T) (=DSM 44213T) producing (S,S)-N,N'-ethylenediaminedisuccinic
RT   acid.";
RL   J. Biotechnol. 189:46-47(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP008953; AIG77225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075V356; -.
DR   STRING; 208439.AJAP_21835; -.
DR   KEGG; aja:AJAP_21835; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_009935_0_0_11; -.
DR   Proteomes; UP000028492; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006558; LamG-like.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIG77225.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..840
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001710311"
FT   DOMAIN          699..831
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   REGION          48..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  91464 MW;  71DD4A055E934B73 CRC64;
     MLPTLSPQRP RRPRRFRKSL TAAVVALTAL ASTPGAATAA ESGWKMGKPR LTTPWTNQVS
     PTNALPEYPR PQLVRENWQN LNGVWEFAGA APGEVPPFGE KLAEKILVPY PTESALSGIQ
     RHEDFMWYRR TFTVPRNWNV GKDNTLRINF GAVDYKAKVY VNGKEVAAHQ GGYGAFSADV
     TSALKPQGEQ EIIVGVEDRT DATWQPVGKQ RRVPDRGIFY EGASGIWQTV WMEPVAAKHV
     GTLGMVPDLK SSTLKLTVDT GGNSGLTVEA VVRDGRKVVS RSKASAAGTI SLPVPQAKLW
     SPDSPFLYDL DVELKDGRRT VDKVSSYFGM REFGTAKGAD GKLRFTLNGK ILFLQSTLDQ
     GYWPDGIYTA PTDQALRFDL EQHKVLGFNT VRKHIKTEPD RWYHHADKLG LLVWQDMPSM
     RTGGRPPVDA QRQFKAELKE LVDQKKNWTS IVGYVPFNEG WAEWSREETG QVAESVKAQD
     PTRLVNAHSG VNCCDSLGDS GKGDVLDWHS YPGPAKPMPD AKRISIDGEH GGYGLEVQDH
     MWFGEGHAYE MVKDQATLNS RYVQNQRDVL ASAQSCGISG SIYTQITDVE HEVNGFFTYD
     RQVKKMDFAQ VRAVNQAIIR NADGSGSGAP DPGPGTPGID GVHAYKFDEG TGSSAKDSVG
     TAHATLTNAQ WAGGVEGGAL AFAGNGQADT GANLVNTAGS YSVSAWAKLD EASGAFQTVV
     SQDTGRDSAF FLQYSGQDQR WAMSFVGLRA LSPEKPEVGR WYHLTGVRDA KAGTLSLYVD
     GAKVASQNAC SAAPSTGHTV IGRGQYGGQQ VDFLRGAVDD VRLYDRPLSD AEVATLAKRD
//
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