ID E2Q9E6_STRCL Unreviewed; 506 AA.
AC E2Q9E6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Glycosyl hydrolase family 109 protein {ECO:0000256|ARBA:ARBA00016631};
DE Flags: Fragment;
GN ORFNames=SCLAV_0490 {ECO:0000313|EMBL:EFG05566.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG05566.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG05566.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000256|ARBA:ARBA00009329}.
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DR EMBL; CM000913; EFG05566.1; -; Genomic_DNA.
DR AlphaFoldDB; E2Q9E6; -.
DR STRING; 1901.BB341_25420; -.
DR eggNOG; COG0673; Bacteria.
DR OMA; MESGKHA; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFG05566.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 110..234
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 247..414
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 506
FT /evidence="ECO:0000313|EMBL:EFG05566.1"
SQ SEQUENCE 506 AA; 54997 MW; 35F0B03134317D64 CRC64;
MTTGRRTPSA ALVGGSMNDA VTPGSDPSGP PGRSAGPGPG PGGDSPAPSR RTVLRTTTGV
AGASLALGAL GTGPAAAAPA GTTEAQATAA APPRKGRTMA GVPFQRRSTV RVGIIGLGNR
GGSMIDLFLV QPGVRVVALC DPVRAKAESA AAKVVAAGQP APALYTKDED DYENLCARGD
LDFVYVATPW EQHFAQARAA MLNGKHVGVE CPVAMRLDEL WALVDLSERT RRHCMQLENC
CYGRNEMRVL RMAHAGLFGE LLHGAGAYNH DLRELMFSPD YYEGPWRRLW HTRLRGDLYP
NHGFGPVANY MDVNRGDRVV SIASFGTPAL GLAEYREAHM PPGDPSWKET YIGADRTVSM
LRTEKGRIIR LEHDVSTPHP YSRINSLGGT KGVFEDYPAR IYVEPDHTDH RWGDFSRYAQ
WDHWLWKEHA NPPGGHGGMD YIMVFRLMQS MRLGLVPDFD VYDAATWTAP VPLSHASLRA
QGAPLPVPDF TRGEWRKPRA GMDSDK
//