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Database: UniProt
Entry: Q1AUD2_RUBXD
LinkDB: Q1AUD2_RUBXD
Original site: Q1AUD2_RUBXD 
ID   Q1AUD2_RUBXD            Unreviewed;      1063 AA.
AC   Q1AUD2;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:ABG04996.1};
DE            EC=3.2.1.24 {ECO:0000313|EMBL:ABG04996.1};
GN   OrderedLocusNames=Rxyl_2051 {ECO:0000313|EMBL:ABG04996.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04996.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG04996.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CP000386; ABG04996.1; -; Genomic_DNA.
DR   RefSeq; WP_011565011.1; NC_008148.1.
DR   AlphaFoldDB; Q1AUD2; -.
DR   STRING; 266117.Rxyl_2051; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   KEGG; rxy:Rxyl_2051; -.
DR   eggNOG; COG0383; Bacteria.
DR   HOGENOM; CLU_003442_0_1_11; -.
DR   OrthoDB; 9772207at2; -.
DR   PhylomeDB; Q1AUD2; -.
DR   Proteomes; UP000006637; Chromosome.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABG04996.1};
KW   Hydrolase {ECO:0000313|EMBL:ABG04996.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT   DOMAIN          543..621
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1063 AA;  117338 MW;  1E9F1C66397ECF11 CRC64;
     MDDRDRQRLE RFVRRIGDLR LWRNALESPV ERWLFSAGGG GAWEPVSLGD RWPRVETPVL
     LRAEARVPED WAGRPVELEL WLGGEGFVRL SNGVTGGLNP FHRSFPVARE ARGGERVGVE
     AEVVSKGLFG SRVSEPRLSR AALVVPEEEV RALELDLSVV AEACLALGGH DAAARLLDVL
     QEAFARLGRR WPTATETVVA RHLLGYRDPL GEVARALPGP YAEKVTDLGL GPEPWSLPSP
     PRPLEPLPEG AREAVREARR AVAEGLAGLR GEHPPAGRVA LTGHAHLDLA WLWPLEEARR
     KARRTFASVL GLMDRYGEFA FNQSSAQMYA WVEEDDPGLF ARVRERVREG RWEPVGGSWV
     EPDCQMPSGE SFVRQLLHGQ RYFERRFGRR CSVAWLPDSF GFSPGVPQLL RGAGIRGFFT
     YKLNWNETDR FPHDLFVWEG LDGSRVVAHS FDNPGIDYNG DVVPHDLLGT WRNFRGKRHH
     PETLFSFGWG DGGGGPSERM LEAYGRLKEF PALPRLRMAR VEEFFSALPE EGLPRWVGEL
     YLELHRGTLT TQGEIKRLNR RAEHRLLEAE AFCALAALRR GAPYPAEELG RLWRTLLLNQ
     FHDILPGSSI REVCEEARRQ LEGVVSGAAG LRGRALRGIS GGGAGSSWAV ANAALWPRPL
     SVVLPGAGCE GVEDLSGEPL PAQRVEEGLL VHDPGRRVPG LGWTGLRPSG RRGGARETVR
     AEGSGGGAVL ENALLSAEIG EGGALLRLYD REAGREVLAG PANRLVAYAD RPREWEAWDI
     DADYAAEGEE LPPASVEVAE EGPLRASVRA ERRWRGSRVA QTYRLLAGSR RLDIETEIDW
     HERRMLLRAL FPVGVRSHEA AFETMYGAVR RPTHRNTSWD AARFEACAHR FCDLSEPGYG
     VALLNDGRYG HSAEDNVLGI SLVRGPLYPD PLADEGTHRF TYSLFPHPGD WTQAGVVEEA
     FALNSPLFAA EGAPPEAAGL VEAEGLPLAL GALKRAEEGE GLVLRLYEPR GARGRAVLRL
     DPPPSRVRRT NLLEEPGEEV ALEGGRVSLE VQPFEVVSLL LEA
//
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