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
//