ID A0A021VUY6_9CELL Unreviewed; 524 AA.
AC A0A021VUY6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:EYR64976.1};
GN ORFNames=N866_19600 {ECO:0000313|EMBL:EYR64976.1};
OS Actinotalea ferrariae CF5-4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Actinotalea.
OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR64976.1, ECO:0000313|Proteomes:UP000019753};
RN [1] {ECO:0000313|EMBL:EYR64976.1, ECO:0000313|Proteomes:UP000019753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR64976.1,
RC ECO:0000313|Proteomes:UP000019753};
RA Chen F., Li Y., Wang G.;
RT "Actinotalea ferrariae CF5-4.";
RL Submitted (JAN-2014) 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:EYR64976.1}.
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DR EMBL; AXCW01000009; EYR64976.1; -; Genomic_DNA.
DR RefSeq; WP_034221785.1; NZ_AXCW01000009.1.
DR AlphaFoldDB; A0A021VUY6; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000019753; 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:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000019753}.
FT DOMAIN 334..520
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 126
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 524 AA; 56359 MW; 93DA4F8DF2EDF968 CRC64;
MTTVRNPILP GCHPDPSICR VGDTYYLVTS TFEYLPGLPV FRSHDLATWE QVGHVVDRPG
QLDYAGIASS GGLYAPTLRH HGGLFWLVCT LVDQDDDARG GNFLMTAEDA AGPWSDPVWL
GVSGIDPSIF FDDDGRAWVH GTRLARDPEW FHQTEVWVRE LDLERRTLVG PEHVVWTGAL
KGAVWAEGPH LYKVDGTYYL LAAEGGTEIH HAVSVARADV ITGPYEGNKG NPVLTHRDLG
RGADVVGVGH ADLVRTPDGD WWAVLLGMRP YGGYHYNLGR ETFLVPVSWE DGWPVFAPGT
ARVTPTVDVP TAGPPPAGGA GVGDASGVVP SGDLRWTAVR ALPEDVAVRR DEGWVLPLRP
ATLADVDVPS FVGLRQQHRD VDVRAVLEAA PGPGQEVGLA VRQSEQHHVL LHVTGDQDGR
SAGRRRAVAV RVAGSERTVL GEVPLQGDSD RVTLTVSARG QDYALGVQEE GRSPVLVATA
DGRWLDSVTT GGFLGLWIGV YATSGGRPST STATVVRVEY VPLD
//