G1092_AKKM8
ID G1092_AKKM8 Reviewed; 473 AA.
AC B2UQL7;
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 2;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=Amuc_0920;
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; ACD04752.1; -; Genomic_DNA.
DR RefSeq; WP_012419967.1; NC_010655.1.
DR PDB; 6T2B; X-ray; 2.13 A; A/B/C/D=27-473.
DR PDBsum; 6T2B; -.
DR AlphaFoldDB; B2UQL7; -.
DR SMR; B2UQL7; -.
DR STRING; 349741.Amuc_0920; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR PRIDE; B2UQL7; -.
DR EnsemblBacteria; ACD04752; ACD04752; Amuc_0920.
DR KEGG; amu:Amuc_0920; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_046965_0_0_0; -.
DR OMA; ENCCYDP; -.
DR OrthoDB; 1465613at2; -.
DR BioCyc; AMUC349741:G1GBX-994-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 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; NAD; Reference proteome; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..473
FT /note="Glycosyl hydrolase family 109 protein 2"
FT /id="PRO_5000370607"
FT BINDING 77..78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256..259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:6T2B"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 326..337
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:6T2B"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:6T2B"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 389..401
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:6T2B"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:6T2B"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:6T2B"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:6T2B"
SQ SEQUENCE 473 AA; 51825 MW; A7F4E017445297C3 CRC64;
MSIFSSRRQF LKSLGLAAGA AAAGNALPGK AVEIPAGDHL WKSASPAAPR PSGSTYMGGF
KAPRLGRIRL AFIGVGGRGF SHLAQMCVMD GVEIVGICDL KEELTKRGVD RVLSRMGKSP
LGYSGGDMEY LTMLKELKPD AVIISTDWSS HARIACDSMK HGAHAFVEVP LAVSLEELWS
LVDTSEATRK HCMMMENVNY GRDELMFLNM VRQGVIGDLL HGEAAYIHCL VTQLGDTRGE
GAWRPEYHTR INGNLYPTHG LGPVAQYMNL ERGEDRFCRV AAFASPALGR NAYAKKHLPA
DHRWNNTPFI CGDMNTAVVK TQLGRTILVQ LDETSPRPYS RANLIQGTEG TLAGFPTRVA
GEKLGNGNYH EWIEGREKLA AIYEKYDHPL WKRIGELATK MGGHGGMDFV MLSRIVECLR
NGEPMDQNVY EGASWSSLLP LTARSIAQGG MPVEFPDFTR GDWKTTMPLA VVS
