ID   G1091_AKKM8             Reviewed;         481 AA.
AC   B2UL75;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 1;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Amuc_0017;
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC   107961 / Muc;
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
CC   -!- FUNCTION: Glycosidase. {ECO:0000250}.
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; CP001071; ACD03864.1; -; Genomic_DNA.
DR   RefSeq; WP_012419079.1; NC_010655.1.
DR   AlphaFoldDB; B2UL75; -.
DR   SMR; B2UL75; -.
DR   STRING; 349741.Amuc_0017; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ACD03864; ACD03864; Amuc_0017.
DR   KEGG; amu:Amuc_0017; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_0; -.
DR   OMA; MESGKHA; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; AMUC349741:G1GBX-19-MON; -.
DR   Proteomes; UP000001031; 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   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           30..481
FT                   /note="Glycosyl hydrolase family 109 protein 1"
FT                   /id="PRO_5000370243"
FT   BINDING         84..85
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         264..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  53803 MW;  1019205F9C30274F CRC64;
     MDNSSSRRRF LQTLGLATGA LAAGSFANAQ EVAPLAPKKI TIPDPNNIGP MTTWPPRKPG
     AIYMGGFRAP KLDKVRVAFV GVGERGSMHV GQMAVIEGAE IVGICDLYED WAKRSADVVE
     KKTGKRPPIF TKGPEDYKRM MKEVKPDAVI VCPSWEWHCR VTCDVMKMGA HAFVEVPMAV
     SIKELWEIVD TSEETRKHCM MMENVNYGRE ELMYLNMVRQ GVIGDLLYGE AAYIHELRGQ
     MKQVERGTGS WRTYHYAKRN GNVYPTHGLG PIAQYMNLAR KDDCFGRLVS FSSPALGRAA
     YAKKNFPADH KWNKLDFACG DMNTSIIKTT MGRTVLVEWD ETSPRPYSRL NLIQGTLGTL
     AGFPTRVAGE KLGNGNYHEW IEGKEKLAPI FEKYDHPLWK RIGPLALKMG GHGGMDFVML
     FRIIECLRNG EPMDQNVYEG AFWSSVSELS EYSVAQGGMP QVFPDFTRGD WKTTAPLGIV
     Q