ID A0A0S9CH96_9SPHN Unreviewed; 515 AA.
AC A0A0S9CH96;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:KQN93004.1};
GN ORFNames=ASE95_10455 {ECO:0000313|EMBL:KQN93004.1};
OS Sphingomonas sp. Leaf231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN93004.1, ECO:0000313|Proteomes:UP000051427};
RN [1] {ECO:0000313|EMBL:KQN93004.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN93004.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN93004.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN93004.1,
RC ECO:0000313|Proteomes:UP000051427};
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, ECO:0000256|RuleBase:RU361187}.
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:KQN93004.1}.
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DR EMBL; LMLS01000002; KQN93004.1; -; Genomic_DNA.
DR RefSeq; WP_056635324.1; NZ_LMLS01000002.1.
DR AlphaFoldDB; A0A0S9CH96; -.
DR STRING; 1736301.ASE95_10455; -.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000051427; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000051427};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006651060"
FT SITE 174
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 515 AA; 56165 MW; 7E7AB5E4B882463B CRC64;
MKPIRAAMMA ALPAIVLAQD RSPVTAPGNP ILADGRYYST DPAPVVNGDT LWILAGRDEA
PAGVNDFIMN EWQLLSTQDP ASGRWRHHPA IAKPEAVFPW AEPGRAYAGQ IVKGPDRRFY
LYAPVLQRVS AAQDRFAIGV AVADRITGPW RDAHPAGPIA SQLMPVRNDI QNIDPTVLID
GDGRVYMYWG TFGQLRGVEL ARDMVTLKGR PVSVDKLTGF FEAPWLMKRR GTYYMLYAGN
NAGPDSPCTP ALYHACIAYG TASSPLGPWT WRGTVLKPVS STTSHAGAVE FRGQWYLAYH
TADAVGGGHF RRSVAIDRME WDDGVFPAAI RPVTPTRRPV ASPAPTRNIA AAAQAHASNE
PVPVQYWMKA LNDGMVKDAP LPPDLWGSWS PQNPPQQWIE YRWSQPVTLD GSRIQFWADH
PAGSTEGVAP PARWRLEYWD GRWKPVRGVS SYGTAPGTWQ TLRFPAIATR CLRAVLDASG
AGTRHAGLAV QEWEALAPRA AVPKGLAAET VAACG
//
