ID A0A1C6SYC8_9ACTN Unreviewed; 458 AA.
AC A0A1C6SYC8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SCL34322.1};
GN ORFNames=GA0070616_4939 {ECO:0000313|EMBL:SCL34322.1};
OS Micromonospora nigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL34322.1, ECO:0000313|Proteomes:UP000199699};
RN [1] {ECO:0000313|EMBL:SCL34322.1, ECO:0000313|Proteomes:UP000199699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL34322.1,
RC ECO:0000313|Proteomes:UP000199699};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FMHT01000003; SCL34322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6SYC8; -.
DR STRING; 145857.GA0070616_4939; -.
DR Proteomes; UP000199699; 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; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
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; PF05270; AbfB; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF110221; AbfB domain; 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:UP000199699};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..458
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008746203"
FT DOMAIN 325..456
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 458 AA; 50368 MW; CD628296B9B1D430 CRC64;
MTRTAFRRVA AYLVAACVAV TAALVATPAQ AANPIVNRFA ADPSMLVAND RMYIYATDDQ
GNSGTYWDSD AWRVYSSSNL VDWTDHGAPF AVGGFSWARQ YAWAPSAVRR NGYYYLYLPV
DRTKIGVARS TSPTGGFSDP RGTPLIERGR DANTGEEPID PAAFVDDNGQ AYLYFGGARA
PKVVRLNADL TSTSGAIQNI TISGTGSGTA FGEAGFVHKR NGLYYYSYST GWPGRIAYAT
ATNPLGPFTY RGIVLDYTNN NTNHHSIAEF NGRWYIAYHR NDLPGSNNFR RSLAMEYLTY
NSDGTIRPVT QTSVGVGTPT SPANRLQSYN FTDRYVRHVD YDARIDANVS PLADSQWRIV
PGLASSADGN VSLESVNFPG YYLRHANYDF VLAQNDNSAT FRADATFKRV PGLADAAAVS
FRSYNFPDRY LRHSNYLLRL DPITDATGRA DATFRITS
//
