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Database: UniProt
Entry: F7PMA6_9EURY
LinkDB: F7PMA6_9EURY
Original site: F7PMA6_9EURY 
ID   F7PMA6_9EURY            Unreviewed;       688 AA.
AC   F7PMA6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Alpha-glucuronidase protein {ECO:0000313|EMBL:ERJ05540.1};
DE   SubName: Full=Alpha-glucuronidase, family GH67 {ECO:0000313|EMBL:CCQ32872.1};
DE            EC=3.2.1.139 {ECO:0000313|EMBL:CCQ32872.1};
GN   Name=aguA {ECO:0000313|EMBL:ERJ05540.1};
GN   ORFNames=HLRTI_002518 {ECO:0000313|EMBL:ERJ05540.1}, HTIA_0732
GN   {ECO:0000313|EMBL:CCQ32872.1};
OS   Halorhabdus tiamatea SARL4B.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ32872.1, ECO:0000313|Proteomes:UP000015381};
RN   [1] {ECO:0000313|EMBL:ERJ05540.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05540.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=21705593; DOI=10.1128/JB.05462-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT   a deep-sea anoxic brine lake.";
RL   J. Bacteriol. 193:4553-4554(2011).
RN   [2] {ECO:0000313|EMBL:ERJ05540.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05540.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
RN   [3] {ECO:0000313|EMBL:CCQ32872.1, ECO:0000313|Proteomes:UP000015381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC   SARL4B {ECO:0000313|EMBL:CCQ32872.1};
RX   PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA   Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA   Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA   Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA   Golyshin P.N., Teeling H.;
RT   "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT   identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT   lake as potential polysaccharide degrader.";
RL   Environ. Microbiol. 16:2525-2537(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC       {ECO:0000256|ARBA:ARBA00008833}.
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DR   EMBL; HF571520; CCQ32872.1; -; Genomic_DNA.
DR   EMBL; AFNT02000031; ERJ05540.1; -; Genomic_DNA.
DR   RefSeq; WP_008527207.1; NZ_AFNT02000031.1.
DR   STRING; 1033806.HTIA_0732; -.
DR   GeneID; 23797934; -.
DR   KEGG; hti:HTIA_0732; -.
DR   PATRIC; fig|1033806.12.peg.725; -.
DR   eggNOG; arCOG13141; Archaea.
DR   HOGENOM; CLU_007125_1_0_2; -.
DR   OrthoDB; 165718at2157; -.
DR   Proteomes; UP000003861; Unassembled WGS sequence.
DR   Proteomes; UP000015381; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR037054; A-glucoronidase_C_sf.
DR   InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR   InterPro; IPR011099; Glyco_hydro_67_C.
DR   InterPro; IPR011100; Glyco_hydro_67_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR   PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR   Pfam; PF07477; Glyco_hydro_67C; 1.
DR   Pfam; PF07488; Glyco_hydro_67M; 1.
DR   Pfam; PF03648; Glyco_hydro_67N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCQ32872.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCQ32872.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   DOMAIN          9..131
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          135..463
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          464..686
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
SQ   SEQUENCE   688 AA;  79186 MW;  E67884912DADEAA0 CRC64;
     MPRNQYDDCW LRYDRVSDDR RESYRRRIKH AYVAEESPEC SAVRDELREA IPGLLGEDVH
     LWQHRPETVD GFLAIGTPGD MEVIKESIPD GAVDDLDDDG YLIRSVEYEG QDCLVVTSGA
     DQGLVYGTFH LLRLLNMGEP IDEIDVREEP AYANRVINHW DNPFRRTVER GYAGESIFDF
     DRLPDLRDRY EDYARLLASL GINGVVLNNV NTEYYPRGST NEASQQFDGW RLLESRRLED
     LTSLASVFRR YGIQIYLSVN FGAPKRIGDL DTFDPLDEDV RQWWREKADE IYDLIPDFGG
     FLVKADSEGQ DGPYNYDRDH VEGANALAQA LEPHGGRVWW RAFVYGSHED RAIQAYDTFE
     PLDGDFAENV TVQIKNGPID FQPREPVSTL FGAMPETDLG LELQITGEYT GQGVHATSHL
     PMWKEIFEFD THADRDGSRV QDFFRGDGEG VVGVTSIGED HTWTGHYLMQ SNLYAFGRLI
     WDPDLDAETI TDEWITQTFG ADEAVLDTVR EILLDSWEAC IDYETGGLGL IHMMHNGQEY
     LENHYYPAPE EWPGYHGATE EGIGYDRTAT GSGYAQQFRD PVASRFEDVE TCPEKHLLFF
     HHLPWDHELE DGTTVIQRLY DNFYDGVEEA ERLRDLWMTL EGKIDDRRFE HVATRFDEQV
     HQAEKWRDVI TGYFYDFAEI EGEKGRVP
//
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