GenomeNet

Database: UniProt
Entry: D9T722_MICAI
LinkDB: D9T722_MICAI
Original site: D9T722_MICAI 
ID   D9T722_MICAI            Unreviewed;       503 AA.
AC   D9T722;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ADL46062.1};
DE            EC=3.2.1.55 {ECO:0000313|EMBL:ADL46062.1};
GN   OrderedLocusNames=Micau_2523 {ECO:0000313|EMBL:ADL46062.1};
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS   129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL46062.1, ECO:0000313|Proteomes:UP000001908};
RN   [1] {ECO:0000313|EMBL:ADL46062.1, ECO:0000313|Proteomes:UP000001908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC   {ECO:0000313|Proteomes:UP000001908};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) 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   ---------------------------------------------------------------------------
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; CP002162; ADL46062.1; -; Genomic_DNA.
DR   RefSeq; WP_013285691.1; NC_014391.1.
DR   AlphaFoldDB; D9T722; -.
DR   STRING; 644283.Micau_2523; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   KEGG; mau:Micau_2523; -.
DR   eggNOG; COG3940; Bacteria.
DR   HOGENOM; CLU_009397_2_1_11; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000001908; Chromosome.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   CDD; cd18817; GH43f_LbAraf43-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; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 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   Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ADL46062.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ADL46062.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT   DOMAIN          373..501
FT                   /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05270"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        246
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            184
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   503 AA;  55431 MW;  104610C6FBCD1E98 CRC64;
     MSPRHLLHPA RRTAADPART ADPARRRLRP ILAAALAMLT ASAGLTAPGP AQAAPAVNYA
     NPLVDQRADP HIVRHTDGYY YMTATVPQYD RIVLRRATTL QGLATATETT IWRRHTSGEM
     GAHIWAPEIH FINGRWYVYF AAGRTDDVWR IRMYVLENAS ANPLTGSWTE RGRITTPWDT
     FSLDASTFVV NGVRYLTWAQ QEPGIATNSN VYLARTGAEP WQITGPVARL VVPAYDWETR
     GYRVAEGPAV IQRNGRVFLT YSASATDANY CLGMLTASAG ANLLDPASWS KSPTPVFASN
     AATGQYGPGH NSFTVSEDGQ SDILVYHDRN YRDISGDPLN DPNRRTRIQK LYWNADGTPN
     LGIPVPDGAT PVRLRSHDLP AAYVRHYDYR ARVEPNVTNL ADSQFRLVPG LAGAGSVSLE
     STNFPGYYLR HRAFALYVER DDGSALFDGD ASFQRRPGLA TTEGLSLESQ NYPGRYVRHR
     DGLLQLETVG TGADRAAATF HLE
//
DBGET integrated database retrieval system