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Database: UniProt
Entry: M3AAX8_STRMB
LinkDB: M3AAX8_STRMB
Original site: M3AAX8_STRMB 
ID   M3AAX8_STRMB            Unreviewed;      1000 AA.
AC   M3AAX8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:EMF02349.1};
GN   ORFNames=H340_00834 {ECO:0000313|EMBL:EMF02349.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EMF02349.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EMF02349.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EMF02349.1,
RC   ECO:0000313|Proteomes:UP000011740};
RX   PubMed=23558536;
RA   Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT   "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT   mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT   Transglutaminase.";
RL   Genome Announc. 1:E0014313-E0014313(2013).
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:EMF02349.1}.
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DR   EMBL; AORZ01000002; EMF02349.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3AAX8; -.
DR   STRING; 1223523.H340_00834; -.
DR   PATRIC; fig|1223523.3.peg.176; -.
DR   eggNOG; COG0383; Bacteria.
DR   Proteomes; UP000011740; 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:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          505..583
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1000 AA;  110028 MW;  CB62E040B81F747A CRC64;
     MDERIRPAVY PESVPLTVGV WHAPGEPVPV AEGLAAPREP IGPGDAWGPA WGTSWFTVTG
     TVPAAWAGRT VEALLDLGFD PNLTGFQCEG LVYRADGSPV KGLNPRNQWV RIGAPVAGGE
     EVRLHVEAAA NPVILDYEPF RPTELGDLAT ADRRPRYRLG RMDLAVFDAV VWELVHDLEV
     LDGLMTGLPE ESPRRWEVLR AVERALDAVD LQDVGGTAAR ARELLADALS APAQASAHRI
     SAVGHAHIDS AWLWPLRETV RKVARTTSNM TALLDEEPDF VYAMSQAQQF AWVKEHRPEV
     WARVKKAVAD GRFVPVGGMW VESDTNMPGS EALARQFTHG KRFFLEEFGI ETEEVWLPDS
     FGYSAALPQL VRLSGSKWFL TQKISWSKTN TFPHHTFWWE GLDGTRVFTH FPPIDTYNAQ
     LSGEELAHAV RNFREKGGAT RSLAPTGWGD GGGGTTREML ARARRLADLE GSARVVFERP
     SAFFEKAHAE YAADAPVWAG ELYLELHRAT LTSQARTKQG NRRAERLLYE AELWSATAAV
     RTGFPYPYER LDRLWKTVLL HQFHDILPGT SIAWVHREAA ATYAAVAAEL ESLVADALAA
     LAGDGSAGGT VVFNAAPHGR ACVAARSARP ADELPRPAPT TATARESGGY VLENGLLRVE
     VDARGLVVSV IDKETRRETI PPGAAANLLQ LHQDFPNMWD AWDVDRFYRN TVTDLTDVQS
     MELTDDGAVR VVRAFGASRA EQRIALPDGL RRVDFTTEVD WHETEKFLKA AFPLDVHADR
     VAAETQFGHL YRPAHTNTSW EAAKFEACAH RFVHVEEHGW GVALVNDSTY GYDVTRTART
     PDSSAPGATT TLRLSLLRAP RFPDPRTDQG AHRFGYALVP GARIDDAVCE GHRVGIPERR
     VPGDRGTPSL VRVDDEAVVV SAVKLSDDGS GDVVVRLYES LGGRARTAVA FDFPTTTVHR
     CDLLERPLGE VESTEHGVSL ELRPFEIVTL RARRDSPSDV
//
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