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Database: UniProt
Entry: A0A0M2HGA3_9MICO
LinkDB: A0A0M2HGA3_9MICO
Original site: A0A0M2HGA3_9MICO 
ID   A0A0M2HGA3_9MICO        Unreviewed;       483 AA.
AC   A0A0M2HGA3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Intracellular exo-alpha-L-arabinofuranosidase 2 {ECO:0000313|EMBL:KJL43324.1};
DE            EC=3.2.1.55 {ECO:0000313|EMBL:KJL43324.1};
GN   Name=abf2 {ECO:0000313|EMBL:KJL43324.1};
GN   ORFNames=RS81_00929 {ECO:0000313|EMBL:KJL43324.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL43324.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL43324.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL43324.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL43324.1}.
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DR   EMBL; JYIZ01000038; KJL43324.1; -; Genomic_DNA.
DR   RefSeq; WP_045274890.1; NZ_JYIZ01000038.1.
DR   AlphaFoldDB; A0A0M2HGA3; -.
DR   STRING; 92835.RS81_00929; -.
DR   PATRIC; fig|92835.4.peg.948; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000033956; 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:KJL43324.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJL43324.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT   DOMAIN          291..474
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   483 AA;  54199 MW;  5200F6DE0563243A CRC64;
     MIDLSASAST HRIDRRVYGQ FAEHLGRCIY EGVWVGADSG IPNKNGIRTD VVDALRHIKV
     PLVRWPGGCF ADEYHWLKGV GDERQPMVNT HWGGVVESNE FGTHEYFELL DQLDAEAYIN
     GNVGSGTVAE MQDWVEYMTL DHTAPMAELR KRHGREQPFK LEFFGVGNES WGCGGNMLPL
     HYANQYRQFQ TYVRNYGDNR ISKIACGANS DDYEWTEVLM ARAAGHMDGL SLHYYTLPTG
     DWDAKGSATD FDEHGWYETI RQTRRMDELL TRHSAIMDTY DPAKRVSLIV DEWGTWYDVE
     QGTNPGFLYQ QSTMRDALVA ALNLNIFHRH GARVRMANIA QMVNVLQAML LTDGSRMVKT
     PTYHVFDLYS DHQDADFVGL PGGGAGAFDS HGDVTVSRKD GALTISTANW HLERGIDAAF
     DLPANVTEVL RAEVLTSAAP TVHNTFDAPD AVRPVELPVR IDGRTLRFEL PPRSVATVRV
     GQR
//
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