ID A0A371JFS7_9FIRM Unreviewed; 1055 AA.
AC A0A371JFS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:RDY31601.1};
GN ORFNames=CG710_009055 {ECO:0000313|EMBL:RDY31601.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY31601.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY31601.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY31601.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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:RDY31601.1}.
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DR EMBL; NOKA02000013; RDY31601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371JFS7; -.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000216411; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd10789; GH38N_AMII_ER_cytosolic; 1.
DR Gene3D; 2.60.40.2220; -; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000216411}.
FT DOMAIN 519..598
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1055 AA; 123131 MW; 533E76187B1C1B27 CRC64;
MNQYKNRIQT ILKSLDKLRY SNVKWVENIY VKEGDYSFAE SYQANLVDYK PFLRGETWGG
TDKHFWFYTV LKITKEYQNH PIIIQLNTGA TDIWNTDNPQ IIVYSNGNMR CAMDMNHNQI
ILTEEETRNQ EIEFAFYAYS NSAENSNFFD LQIAACHTDV EELYYDMKVL FDAVCLLRED
DIEAIKTLEK LGQCVNLLDL RDTDKQEFFA SVKEADSFLK DNFYLNKSEK PEVIVHSIGH
THIDVAWKWQ LKQTRQKVVR SFLTVLNLMD RYPEYKFMSS QPQLYQFVKE EAPQLYERIK
EKVLEGRWET EGAMWLEADC NLASGESLIR QLLYGKRFFK EEFGVKRQEV LWLPDVFGYS
VALPQIMKKS GIRYFMTTKI GWNEYNQIPN DTFYWKGLDG SEILTYFITT KDYEVYPELK
RNPSFNTTYN GRQNASQIKG TWQRYQNKEL NQEVLTCYGH GDGGGGPTAE MLEESKRLEY
GVCGVPATRQ TFAKDFFHTL EANLKGKTVP KWSGELYLEF HRGTYTSMAR NKKNNRECEF
LNVDAEFFSM LALMLGKNYE YPQKELEQAW RLVLLNQFHD ILPGSSIKEV YEDCDQQYGL
VRKLDETIIE EARRNITANL AAADEEEKLV VYNCLSFERT TIVKVDKHKE PITSLLMQES
KDGEYLYLIH NAVSKGMEVF DESNAARNER VLTKSAPFGQ VIESVNEKEA GLSIETKFYL
IQLNKAGEFI SIYDKTARRE VLQATKAGNR LVVFEDRPNE YDAWNIDPYY KEKSWAIDEL
LECRIVENGP IQACIYIKRE FLSSTIEQYI YFYGHTKRID FKTTIDWKQQ QLLLKAEFPV
DIISNKATYE VQFGNVERPT HENTSWDAAK FEVCAHKWAD ISEYGYGVAL LNDCKYGYDI
HESVMRLTLI KSGIFPNPDA DKEIHRFTYS LFPHEGDFRA GKVTQEAYDL NCPLSGEIVK
GIKTNSYSLL RLDAENVFVD VIKQAEDNQD IIIRLYEAYK KRSVIKAESP YFTTGTIWEC
DCMEQPETEI AGKNGEIQFE MKPYEIKTLR IKQNR
//
