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
//