ID E7GBL1_9FIRM Unreviewed; 881 AA.
AC E7GBL1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Alpha-mannosidase/fructosidase {ECO:0000313|EMBL:EFW04581.1};
GN ORFNames=HMPREF9488_02152 {ECO:0000313|EMBL:EFW04581.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW04581.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW04581.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW04581.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFW04581.1}.
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DR EMBL; ADKX01000035; EFW04581.1; -; Genomic_DNA.
DR RefSeq; WP_008789252.1; NZ_WSNW01000001.1.
DR AlphaFoldDB; E7GBL1; -.
DR STRING; 100884.GCA_000269565_02262; -.
DR GeneID; 78230096; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_2_1_9; -.
DR OrthoDB; 9764050at2; -.
DR Proteomes; UP000003157; 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 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; 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:SF2; MANNOSYLGLYCERATE HYDROLASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 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:UP000003157}.
FT DOMAIN 277..355
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 881 AA; 102246 MW; FAAA86CF51AC0B2A CRC64;
MSRIHFIPHV HWDREWLRST DSSRIKLVYF FDRLIDMLEN DPKMYYFTFD GQTAALEDYL
AIQPFQKETI KKLVKERRLF IGPWYVQPDM IIPSGEALVR NLLIGSQYAS SLGHCMNVGW
VPDAFGQNKI TPYLFKELGM KGIYAWRGFD YEVLKDSLFM WKGNGNVKLP TVHFALGYGH
YRGFPEEYEN VKADMQDFIP KLEARFQDQE VLFMLGSDYA FPRKHSSLMI EKLKQEGYDC
QMNNPEDYLE TLLSAAKHNH HVLEEYQGEA RSATLGRIHA GITSTRIDIK NAMRYYETLM
AKVVEPMIAI SRFQGGHCHQ ELVNYFWKII FKNQFHDSIY SSSPESINQT VENRLLNLRH
GLNELIWMNF RYLAESANLS SVQKDEDILV LFNTLPYQRQ DYAFVSMIVK HKDFVLKRQD
GTIVPYQMMN EVIATCHDIE YYNGMENFHD SGEVLEGTKY KIQIKIDASI LPAMGYEILK
VCFHQQNSQE MIGDVQILEN GAENQYLKMF IQKDGTISVE NKKTKEVYHH LNAFVEKGDD
GDEYNYSPCG NDKEISIYHN QPTITCIESS DIEVKYRIEY NAKVPAKVVN HERVQELEAL
KIISDVSLKA RSQTIDFTTT IENHSCDHIV RVTFDDLYQS EENCSQDQFG TIIRKNIIEN
QKSLEDGATE YVLPMYAMQR FVQLHHQKSI MALISKGPLE YEIENNQKIC LTLLRSVGKF
GKADLLIRPG RASGYRMDAP SSQLLNKNIT SEYSLFFGIQ ADMSKMIQDA EMLNTPVQTR
YLNDISRQKN QGLDWQYSAI SLDTRVELMA LKKAEHGQYS VIRIVNNRDN DVENVRFHVP
LTKKCYLSDV QEKKKIELEN KNGEIIIKNI MSNTFVTVII E
//
