ID A0A3A9YVJ9_9ACTN Unreviewed; 717 AA.
AC A0A3A9YVJ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Alpha-glucuronidase {ECO:0000313|EMBL:RKN39594.1};
GN ORFNames=D7223_28235 {ECO:0000313|EMBL:RKN39594.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN39594.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN39594.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN39594.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC {ECO:0000256|PIRNR:PIRNR029900}.
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:RKN39594.1}.
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DR EMBL; RBAK01000016; RKN39594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9YVJ9; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000281726; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
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; IPR011395; Glyco_hydro_67_aGlcAse.
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 PIRSF; PIRSF029900; Alpha-glucuronds; 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|PIRNR:PIRNR029900};
KW Glycosidase {ECO:0000256|PIRNR:PIRNR029900};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW Polysaccharide degradation {ECO:0000256|PIRNR:PIRNR029900};
KW Reference proteome {ECO:0000313|Proteomes:UP000281726};
KW Xylan degradation {ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 167..485
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 486..714
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT REGION 52..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 717 AA; 78670 MW; B8D3E679E96F5459 CRC64;
MSLPGTGTAR WHPAWLPPEA FRAIGTRRVL VHGAGPLVDT VFEEVTRACA DHGGRARRTG
ATPPAGTTDS AGPPDGDGGG GPAADEVDAT QVALVLRGAG ALPAVAGDAP VPAGGEPGAL
GDEGFLLTRD GAVTVLLADA PAGLLYGLFH LVRLGETAFD PARPGAVHRP AVRRRMLDHW
DNVDVHPVMG QVERGYAGGS IFWRDGRARR DLARLRAYGR LLAACGINAI SVNNVNVHAT
EARLLTDRLG DVAEIADVLR PYGVRVHLSV TFAAPVVVGG LATADPRERR VRDWWARTTR
QVYQRIPDFG GYLVKADSEG QPGPFAYGRD HADGANLLAE ALAPHGGVVH WRAFVYDHRQ
DWRDRSTDRA RAAYDHFAPL DGRFDDNVVL QVKYGPMDFQ AREPVSPVIA AMPATRLAVE
FQVTQEYTGQ QRHVCYLGPC WSEVLGFRPW GPDGHRVADV VAGVPDRGRG GDLVAVSNVG
DDPYWTGHPL AQANLYAFGR LAWDPRRDPR AVLDEWIDLT FPPTTTGDPE RVRETLHALL
DDSWRTYERY TAPLGVGFMV SPANRHYGPD VDGYEYSRWG TYHFADRDGV GVDRTRATGT
GFAGQYPQPW STVYESVDEC PDELLLFFHH VPYGHVLRGG STVVQHIYDT HFAGAEEVTA
MRERWRDLAG LVDPALYDRV GERLDEQVRS ATEWRDQINT YFFRKSGVPD AKGRRIH
//
