GH109_STRCO
ID GH109_STRCO Reviewed; 472 AA.
AC Q9RK81;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glycosyl hydrolase family 109 protein;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=SCO0529; ORFNames=SCF11.09c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 23899;
RX PubMed=17401360; DOI=10.1038/nbt1298;
RA Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT "Bacterial glycosidases for the production of universal red blood cells.";
RL Nat. Biotechnol. 25:454-464(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Glycosidase (By similarity). Has no alpha-N-
CC acetylgalactosaminidase activity. {ECO:0000250,
CC ECO:0000269|PubMed:17401360}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC {ECO:0000250};
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000305}.
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DR EMBL; AM039449; CAJ01381.1; -; Genomic_DNA.
DR EMBL; AL939105; CAB59586.1; -; Genomic_DNA.
DR RefSeq; NP_624843.1; NC_003888.3.
DR RefSeq; WP_011027183.1; NZ_VNID01000015.1.
DR AlphaFoldDB; Q9RK81; -.
DR SMR; Q9RK81; -.
DR STRING; 100226.SCO0529; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR GeneID; 1095952; -.
DR KEGG; sco:SCO0529; -.
DR PATRIC; fig|100226.15.peg.509; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_046965_0_0_11; -.
DR InParanoid; Q9RK81; -.
DR OMA; MESGKHA; -.
DR PhylomeDB; Q9RK81; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; NAD; Reference proteome; Signal.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..472
FT /note="Glycosyl hydrolase family 109 protein"
FT /id="PRO_0000348565"
FT BINDING 68..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 159..160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 51800 MW; F32670FD65DC9AA7 CRC64;
MSQTPAVSRR LLLGSAAATG ALATGIGSAA PVAAAEQAPR RRPGQKSMIG VPFAAHPTVR
VAVIGLGNRG GGMITGWAAV PGCTVTAVCD IRADRAERAA DRLESKGNPR PAEYGGSADS
YARMLRRDDI DLVYIATPWE FHYEHGRAAL LSGRHAVVEL PVATELRQLW DLVDTSERTR
RHLLLSENCN YGRNELAMLK AAHDGLFGDL TNGHGGYLHD LRELLFSDTY YTDSWRRLWH
TRSTASFYPM HGLAPIAAAM DVNRGDRMTT LRATTTAPKG LADYRARFVP RDHPSWKETY
INGDLVTCMI ETAKGRTVRA EHDVSSPRPY SRINTLAGSR GIVEDYAGSA PTGARIYVEP
DHGGHTWRDF ETYRKEYDHW LWQKVGDDAA NNGGHGGMDY VLQWRTVQLM RAGLVPDIDV
YDSAAWCSPV PLSVTSLARG GRPVEIPDFT RGAWRERRPG LDSAPTDMPP AG
