ID A0A0Q8Z1Z6_9ACTN Unreviewed; 755 AA.
AC A0A0Q8Z1Z6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=LamG-like jellyroll fold domain-containing protein {ECO:0000259|SMART:SM00560};
GN ORFNames=ASE41_35425 {ECO:0000313|EMBL:KRD00541.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD00541.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD00541.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD00541.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD00541.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD00541.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KRD00541.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMIZ01000054; KRD00541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8Z1Z6; -.
DR STRING; 1736503.ASE41_35425; -.
DR Proteomes; UP000051177; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.2340; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..755
FT /note="LamG-like jellyroll fold domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006364083"
FT DOMAIN 85..225
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 441
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 755 AA; 80400 MW; 8BC4E50535A59227 CRC64;
MTAAALLTGL AGPPAPAQAA EITDGLVLWY KLDATSGTVA VDSSGNGRNG TVNGAAGWSG
SGQGLTFNGS DTYIKVPDDI LSGMNSVSVS MDVQIDAAQA TPYFLYGFGN TAGGAGDGYL
FATGDTLRTA IASGGFATEQ NTRTSTALPR SVWKHVTYTQ TGTTGILYQD GVEVARNPSV
TVTPGAVGSG VTTADYIGKS LYSTDKLFKG RIRDFRVYNR ALAPGEVLAV SGNTTAIAAA
DDASLKIAAL VDDANGKVTL PLKEGTDLTA LAPRFTLSQG ASISPASGTP HDFTQPVTYE
VTGSDGTKRT WTVSAQIMRS PVLPGLTADP NIVRFGDTYY IYPTTDGFAG WSGTRFRAYS
SKDLVHWTDH GVVLDLGPDV SWADSRAWAP TATAKNGKFY LYYSADTNIG VAVSDSPAGP
FKDPLGKPLI ARGSHPGQMI DPDVFTDDDG RSYLYWGNGH AYVVPLNDDM LSFDASKITE
ITPGGYNEGS FVIKRKGAYY LMWSENDTRD ENYRVAYATG SSPTGPWTKR GVILEKDLSL
GIKGPGHHSV VQVPGTDDWY IAYHRFAIPG GDGTHRETTV DKLEFDADGL IKKVVPTLSS
IAPVTGGVTL PTNTTRSLRS VNFPGRYAVV RSDSLGYLDP VTSSSTTAVL QSATFTVVPG
LADGSCYSFR DASGRYLRHK DLRIRADASN GTTLFAKDAT YCARQGSVTG SVGLESYNYP
GRYLRHYDYE LRLDTYQDNA TFRADSSFTP VSPWA
//
