ID   E6TF30_MYCSR            Unreviewed;      1378 AA.
AC   E6TF30;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:ADU01076.1};
GN   OrderedLocusNames=Mspyr1_45210 {ECO:0000313|EMBL:ADU01076.1};
OS   Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS   (Mycobacterium gilvum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=278137 {ECO:0000313|EMBL:ADU01076.1, ECO:0000313|Proteomes:UP000008916};
RN   [1] {ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA   Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU01076.1, ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RX   PubMed=22180818;
RA   Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA   Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT   reclassification to Mycobacterium gilvum Spyr1.";
RL   Stand. Genomic Sci. 5:144-153(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CP002385; ADU01076.1; -; Genomic_DNA.
DR   RefSeq; WP_013472737.1; NC_014814.1.
DR   KEGG; msp:Mspyr1_45210; -.
DR   HOGENOM; CLU_002752_0_0_11; -.
DR   Proteomes; UP000008916; Chromosome.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR011330; Glyco_hydro/deAcase_b/a-brl.
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; 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;
FT   DOMAIN          405..476
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1378 AA;  149224 MW;  6C77DAB0D5C20095 CRC64;
     MDVLSAASTE LFTGPPDAPM QVVRVTYRDC AMPTPVRVEG AGLRTVGEPV AEPGGVSVEV
     SVQVADPAPG RRRDATVVAG DTSAAFDFVD AEPGWTMFMV SHFHYDPVWW NTQAAYTSVW
     TEDPPGRCRQ TNGFELVSAH LDMARRDPEY TFVLAEVDYL KPFWDTHPWE RADLRRLIAE
     GRVEIMGGTY NEPNTNLTSP ETAIRNFVHG IGFQRDVLGA EPATAWQLDV FGHDPQFPGM
     AADAGLTSSS WARGPHHQWG PMAEVDGRAG DPARMQFASE FEWIAPSGRG LLTHYMPAHY
     AGGWWMDSSA TLQEAEDATF ELFTNLKKVA LTRNVLLPVG TDYTPPNKWV TDIHRDWNAR
     YTWPRFVCAL PREFFAAVRA ELDARGGTAS PQTRDMNPIY TGKDVSYIDT KQANRAAENA
     TLEAEQFAVF AGALTGATYP DAALAKAWVQ LAYGAHHDAI TGSESDQVYL DLLTGWRDAW
     QLGTTARDHA LALLSDSVDA SVVVWNPLSH NRCDMVTVRL EEPFTGGMID RDGNAVPVLT
     EHGGRTVTWR ARDVPSLGWQ SYTFVPGDQG GGWEPSEGDE IANDRYRVRV DPARGGGVCS
     LQADGRELVA EGRVGNELTV YAEYPAHPVA GEGPWHLLPR GPVTSSSQHP ATAVRRYRSA
     LGERLVIDGG IPGLFTYTQT LTLWHGVDRL DCRTTVDDFG GSDRLLRLRW PCPITGAMPV
     SEVGDAVIGR GFALLHDPDS GESVDAAVHS HTLDNPAFGW FGLSSALRVR FRGDAVRAVS
     VAEVISPSGC EPAVRKLVAA LARAGVTATC TAADAPRYGD LSIDSNLPDL RISVGGVDEN
     AFTATILTGV VGDPPRWIPA ARPLREVWVP GADLRDPSAL PVLVVGADGD VDDAIAALID
     DLADAQIRID QDVDEHFESY TVAMINRGVP GFAVEADGTL NASLMRSCTG WPSGTWIDPP
     RRTAPDGSNF QLQHWTHAFD YAVVAGEGDW RDLRMPSRAA EFNQPLLPVP ARHDPSRGGL
     PSWGSLLDVA PERDVRVAAL KAHGNPTARG SARRGGPHDG VTLRVVETLG RDAEVSVQSG
     LRHIDAPQRL NLIEEPLRET RRTAHLAGYE IATLRTELNF PRIRNAEQMS LAPDAEPVQP
     LYARYWLHNR GPAPLGGLPA VAHLHPHRLQ AVGSEVVTLR LTVASDATDT ALHGRVRLVA
     PPGWDLGVDE LPFVVPPGEY LESTVEVRVP GDVMPGHYPV RAELALVGGE IPAAWHQTVE
     DVAVISVGGH ADPLLHWVAE PQAVHVDAGQ VASLGITVGS AAHADLTVEA HLISPWGTWE
     WLRPNIVGGA LPARGGLALH FEVAPPVGTA PGRWWALIRV ACAGELLYSP AVPVVVRR
//