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Database: UniProt
Entry: A0A1H5GQL2_9MICO
LinkDB: A0A1H5GQL2_9MICO
Original site: A0A1H5GQL2_9MICO 
ID   A0A1H5GQL2_9MICO        Unreviewed;      1012 AA.
AC   A0A1H5GQL2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:SEE17976.1};
GN   ORFNames=SAMN04488554_1728 {ECO:0000313|EMBL:SEE17976.1};
OS   Ruania alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX   NCBI_TaxID=648782 {ECO:0000313|EMBL:SEE17976.1, ECO:0000313|Proteomes:UP000199220};
RN   [1] {ECO:0000313|Proteomes:UP000199220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNTX01000001; SEE17976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5GQL2; -.
DR   STRING; 648782.SAMN04488554_1728; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000199220; 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; 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:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199220}.
FT   DOMAIN          530..608
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1012 AA;  110842 MW;  876F011601B6BD8D CRC64;
     MTEIRQQDAS TQIVRRLDRA VREVIRPARI RYRSPLTVSA RRVGGEPVSF ADGTRGDLTP
     LAVGDSWGRA WDTVWMHVSG AVPGEWDART AVAAELEIDL GFTTAQSGFQ AEGLVYTTDG
     SVVRALSPLN HRVPLQVGPG AAIEYWVEAA ANPTLNNAHG TNLIPLAHLG SWESAGEEEI
     YRFAGAHVVV PEAEVVALAH DVDLLRGIAT NDGTDVRRRD LILAAIERML AVLDPTDVPG
     TAAAARERLT AVLTTPAHAS AMTLTAVGHA HIDSAWLWPL RETIRKCART FSNVVTLMED
     NPDFVFACSS AQQFAWMKEH YPDLYTRISD AVARGQFVPV GGMWVESDTN MPSGESLVRQ
     FVAGQGFFMR EFGIECPEVW LPDSFGYTGA FPQIARLAGA HWFFGQKMSW NRSNRMPHHT
     FTWEGIDGSR ILTHFTPVDT YNSDLSPVEL GYAHGNFADH ADFSGGIVPF GYGDGGGGPT
     REMLEAGRRA ADVEGLPRVR FGAPSEFFAE AEAEAQDADP ATWTGEMYLE LHRGTYSSQA
     RTKYGNRRAE ALLREAELWA ATASVRAGAA YPQEELARIW ERTLLLQFHD ILPGSSISWV
     HADAERMHGE DRDALEQIIA DALDILAGTG EQTLTVNGAP FPRAGIPPLG GVAEPAPPNQ
     QVSVERSGDR HVLRTSHLEL QVAADGTFVE LLDHASGRSL FSPDAPGNTL DLHQDIPTDW
     DAWDIDAHYR ELTVPADGTA EVRIADDGTP AVHITRTVGA SRVEQVVTLA PDRPVVDIVT
     EVDWHERQRL LKLAHPFRID ARTSAAETQF GHVVRPTHEN TSWDEARFEI VAHRWLHVSD
     GVVGAAVVND STYGHDVARL PAQEYLTQVR QTLLRGPLYP DPESDQGRHT FRTRLVLTPD
     VSGAVDEAYD MDTPLRTARG DGREIAPVAQ AFGDGVVLHT VKLAEDGTGD LIVRVHEAYG
     RPTRARIVVN GAQIRQVDLL ERVLDSDAGP VADQLELDLH AFQIVTVRAR AH
//
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