ID L0ITU7_9MYCO Unreviewed; 1398 AA.
AC L0ITU7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:AGB21377.1};
GN ORFNames=Mycsm_00950 {ECO:0000313|EMBL:AGB21377.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB21377.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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; CP003078; AGB21377.1; -; Genomic_DNA.
DR RefSeq; WP_015304966.1; NC_019966.1.
DR STRING; 212767.Mycsm_00950; -.
DR KEGG; msa:Mycsm_00950; -.
DR PATRIC; fig|710686.3.peg.954; -.
DR HOGENOM; CLU_002752_0_0_11; -.
DR OrthoDB; 1049785at2; -.
DR Proteomes; UP000010844; Chromosome.
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; cd10786; GH38N_AMII_like; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
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 InterPro; IPR013783; Ig-like_fold.
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 Pfam; PF10633; NPCBM_assoc; 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; 2.
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}.
FT DOMAIN 386..464
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1398 AA; 150421 MW; 911AF395C80FF770 CRC64;
MHVISAESTE RFVGPADDPL QLVRVNYTGG VGEIQVEGDG LAGSAKAGPG DGTVEVPVRV
ERPTPGEQRT ARAGDASFVF TVAEPGWTMY MISHFHYDPV WWNTQAGYTS VWSEDPPGRC
RQTNGLELVR AHLEMARREP EYKFVLAEVD YLKPYWDTYP EDRDDLRRFI ADGRVEVMGG
AYNEPNTNLT NAETTIRNFV AGMGFQRDIM GADPRTAWQL DVFGHDPQFP GMAADAGLTS
SSWARGPHHQ WGPVAGGGDP RRMQFSSEFE WIAPSGRGLL THYMPAHYSA GWWMDSSATL
AEAEQATYEL FATLKTVALT RNVLLPVGTD YTPPNKWVTD IHRDWNARYT WPRFVCALPR
EFFAAVQTEL TERGVEASPQ TRDMNPIYTG CHVSYIDTKQ ANRATEDAVL DAERFAVFAG
LLGGATYPHA ALAKAWVQLA YGAHHDAITG SESDQVYLDL LTGWRDAWDL GTTARDNALQ
LLSSAVDGSV VVWNPLAHKR SDVVTARLSR PAGAGVRVLD SEGGELAAHV EHGGRSISWL
ARDVPSVGWQ SYRFASGRSS GWEPLATDEI RNDHYRLSVD PARGGGVSSL VEVASGRELI
ADGRVGNELA VYDEYPAHPQ AGEGPWHLLP KGPVVASSAE AASVQAYRGP LGERLIIDGR
IGDVLRYKQI VTLWHGVARV DCRATIDEFT GEDRLLRLRW PCPVPGALPV SEVGDAVIGR
GFGLLHDSRA GRPATSGQRA EEAVDSAQHP WTLDNPAYGW FGLSSAARVR VGEAVCAVSV
AEVISPTESV SAPLARALMV ALVRAGVTAT CSSADKPRYG DLTVDSNLPD ARIALGGPDQ
NAFTAAVLAD AEPVYAEELK RQLYASGTAR VWVPAVSTLA DQWVPGADLR GVRALPVLIV
AGAELEEVVT SVVDDLADFE IVVEQAVASA VEPFEARTVA VLNRGMPGFA VDSDGTLHMS
LMRSCTGWPS GTWIDPPRRT APDGSNFQLQ HWTHTFDYAL VSGEGDWRQA DIPARSAEFS
RPLLTVVENH GAAGGLPPWG SLLEIEPAGK VALGALKAAG NPLAAGSGQQ VDAADGVAVR
LIETCGATTD VVVRSGLRRI SAASRVDLLE QPRVQGLAAD SLTLHGYEIA TVLTRLNMPQ
VLEADHAVLA PEAEAAQPLY ARYWLHNRGP AALGGLPAVA HLHPQQVEAE PNSQVSLRLT
VATDTSDAAL HGKVRLLCPD GWSADQDELS FVLPPGEYLE TDVAVAVPPQ VQPGLYPLRA
ELAVTGSDAA SIPPSWRQVV EDVCVVSVGA TDEHVLRLVS DPEPIEVSAG ETAQLAVTVG
TDAHVDLAVE AHLISPWGTW EWMGPAAVGR ELPARATVQL AFDVAPPAWV QPGEWWALIR
IGCAGSLVYS LAVKVTVR
//
