ID W0Z8J0_9MICO Unreviewed; 505 AA.
AC W0Z8J0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alpha-N-arabinofuranosidase 2 {ECO:0000313|EMBL:CDJ99479.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:CDJ99479.1};
GN Name=xsa {ECO:0000313|EMBL:CDJ99479.1};
GN ORFNames=MIC448_1510016 {ECO:0000313|EMBL:CDJ99479.1};
OS Microbacterium sp. C448.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDJ99479.1, ECO:0000313|Proteomes:UP000028883};
RN [1] {ECO:0000313|EMBL:CDJ99479.1, ECO:0000313|Proteomes:UP000028883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C448 {ECO:0000313|EMBL:CDJ99479.1,
RC ECO:0000313|Proteomes:UP000028883};
RX PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT Microbacterium sp. Strain C448.";
RL Genome Announc. Announc.2:e01113-e01113(2014).
CC -!- SUBUNIT: Homohexamer; trimer of dimers.
CC {ECO:0000256|ARBA:ARBA00011165}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC {ECO:0000256|ARBA:ARBA00007186}.
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:CDJ99479.1}.
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; CBVQ010000059; CDJ99479.1; -; Genomic_DNA.
DR RefSeq; WP_036299748.1; NZ_HG779731.1.
DR AlphaFoldDB; W0Z8J0; -.
DR STRING; 1177594.MIC448_1510016; -.
DR eggNOG; COG3534; Bacteria.
DR HOGENOM; CLU_017810_2_0_11; -.
DR OrthoDB; 9758333at2; -.
DR Proteomes; UP000028883; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43576:SF2; INTRACELLULAR EXO-ALPHA-L-ARABINOFURANOSIDASE 2; 1.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:CDJ99479.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDJ99479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028883}.
FT DOMAIN 307..496
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 505 AA; 55458 MW; 28DC21713772EED2 CRC64;
MTASARAVID LDVTGHRINR HIYGHFAEHL GRCIYDGFWV GEDSPIPNER GIRLDIVDAL
RALDIPNLRW PGGCFADTYH WKDGIGPRES RPAIANTHWG DVVENNHFGT HEFMDLCDLL
GTDAYVNGNL GSGTVQEMAD WVEYLTRDDD SPMARLRREN GRDEPWKVPF WGLGNEAWGC
GGNMSAGHYA AEARRYATFC RDHGGNTLTR IAAGANEGDL EWTRTLMKSV TECAGCTMGA
EPVYQAISFH FYTHSGTGIN TEDAAGFTTE QYYATLAYAS EIERLIRGHV AVMDSYDPDG
RIGLVCDEWG TWWNVEEGTN PGFLFQQNTV RDALVAGIHF DAFHRHARRI SMANIAQTVN
VLQAMVLTDG DRLVLTPTYH VFEMNKGHQD ASQLSAHLLE APAAPVAGAE LPLLSMSAST
KDAGALISLT HLAVDETLDV SIDLRGRGAH VRRARVLTGD APDAFNAPGE DARVAPTPLE
TTLEGGVLRL QMPPHSFATI ELDLS
//