ID   MANG_DICDI              Reviewed;        1087 AA.
AC   Q54K67;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Alpha-mannosidase G;
DE            EC=3.2.1.24;
GN   Name=manG; ORFNames=DDB_G0287577;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 863-870 AND 932-938, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC         in alpha-D-mannosides.; EC=3.2.1.24;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR   EMBL; AAFI02000102; EAL63688.1; -; Genomic_DNA.
DR   RefSeq; XP_637188.1; XM_632096.1.
DR   AlphaFoldDB; Q54K67; -.
DR   SMR; Q54K67; -.
DR   STRING; 44689.Q54K67; -.
DR   PaxDb; 44689-DDB0231611; -.
DR   EnsemblProtists; EAL63688; EAL63688; DDB_G0287577.
DR   GeneID; 8626190; -.
DR   KEGG; ddi:DDB_G0287577; -.
DR   dictyBase; DDB_G0287577; manG.
DR   eggNOG; KOG4342; Eukaryota.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   InParanoid; Q54K67; -.
DR   OMA; GQYWDAW; -.
DR   PhylomeDB; Q54K67; -.
DR   Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR   PRO; PR:Q54K67; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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   GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..1087
FT                   /note="Alpha-mannosidase G"
FT                   /id="PRO_0000327486"
FT   ACT_SITE        376
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         579
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1087 AA;  123691 MW;  32E15E3EA33F6CAA CRC64;
     MTSGNVMLKH QDVTIERIEK FLSDTYFVRE NLYGKLISLK SSEAVKVKVS PKVEGISYKD
     AIQLEYKDTK IGESFGPSWT NYWFKVTIDV PTDWKDKTIH FIWNSSCEGL IWMNGIAIQG
     LIGGTWQDLR EEYKLIENSK GGEHFEFYIE ISCNGMFGVG KDGLINPCDP DRTFELTKAE
     IRVKNKEANE LYMYLQMLYD VGKNFPKESL RKKQAIWVAN DIINQCNVND SRTFSKCIEL
     AKKEFFSQHN SESQTRVWAV GHCHIDLCWL WSFEKTKEKC ARSFSTQILY MDYYPQFKFT
     QSQAQAYQWT KENYPELYER IKEKVVTGQF IPTGGTWVEM DGNLPSGESF IRQFLYGQRF
     FEKEFGKKCT EFFLPDTFGY SAQLPQVIRH MGIENFITQK LSWNNLNKFP HSTFIWEGID
     GSSVLTHFPP ADTYNSQADV KEIVMSSSNN KDIDRCNESM LLYGNGDGGG GPTIPMIERL
     TILKDTAGIP KIEFSTPAQF FKQLEPHRSK LNKWVGELYF ELHRGTYTSQ ATTKRGNRLC
     EIELHATEML TSYCELFVEG FKSPNLSKLW QQVLLCQFHD ALPGSSIQVC YEDILKIHQQ
     VLVECKNIIT QSMNHITGTL LKIDNLPTTS TTTSTTTTST TECTKNSEFV LAFNANDFEI
     SRVIEIPKSN KDIQAQYINA IQTSYNGLPL GTVSLPPNGF SAINISTSGD NRTINRKPGY
     PCTAIEKNDA SGDILIDNQF ISIVIGSNGR IKSLIEKSAN REVIKQDGSL GNRLIIFDDT
     CLFWDAWDQE IFSLEKPLSI LEGTCKIIEN GPLRCVVQVH YDSKGLPSGN GSVNQTIIVH
     FNSARVDFET NVNWNEAHKL LRVDFDTNIR AKNANYEIQF GHIERPTHYN TSWDFARFEV
     VGHKWADLSE YDFGMALLND CKYGYSTLGG RIGLSLLRSP KSPDDTCDMG SHKFTYSIYP
     HRGSLQSASV IKEGYSLNNN FYISETPFSL ASTTHIDKTF ISTNKEAIIV DTIKKAEDGT
     SFVVRVYESF GGATTFNFTS SILPIPFKSI IECNGLEEVN QSSKSYKFND TIKINPFEIK
     TFRFISN
//