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Database: UniProt
Entry: C5Z7K3_SORBI
LinkDB: C5Z7K3_SORBI
Original site: C5Z7K3_SORBI 
ID   C5Z7K3_SORBI            Unreviewed;      1184 AA.
AC   C5Z7K3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=SORBI_3010G100800 {ECO:0000313|EMBL:EER89512.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EER89512.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EER89512.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   EMBL; CM000769; EER89512.1; -; Genomic_DNA.
DR   RefSeq; XP_002438145.1; XM_002438100.1.
DR   AlphaFoldDB; C5Z7K3; -.
DR   STRING; 4558.C5Z7K3; -.
DR   EnsemblPlants; EER89512; EER89512; SORBI_3010G100800.
DR   GeneID; 8061493; -.
DR   Gramene; EER89512; EER89512; SORBI_3010G100800.
DR   KEGG; sbi:8061493; -.
DR   eggNOG; KOG1958; Eukaryota.
DR   HOGENOM; CLU_004690_1_0_1; -.
DR   InParanoid; C5Z7K3; -.
DR   OMA; GHQWLKY; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000000768; Chromosome 10.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
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:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblPlants.
DR   CDD; cd10809; GH38N_AMII_GMII_SfManIII_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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
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; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 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:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          512..597
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  134639 MW;  37663C672409EFBA CRC64;
     MPFFSGSGGG RSGALLPTTS KPKAHHHLRS KSSLSAPASS RRRGGGLHSA SSPYSRRALC
     LAATAFAALF ILAFLRLGFP SSRSAALSSP ARPRARLTRR PAFRLRDSAA AEAAAAAVAA
     RIGREAPVDI TTRDLYERIE FSDEDGGAWK QGWEVKYRGD EWDAEKLKVF VAPHSHNDPG
     WIRTVEEYYE RQSRHILDTI VESLSKDSRR KFIWEEMSYL ERWWRDATPK KQEAFAKLVR
     DGQLEIVSGG WVMNDEANSH YFAIIEQIME GNMWLNDTIG VIPKNSWSID PFGYSSTMAY
     LLRRMGFHNM LIQRTHYEVK KELAMKKNLE YLWRQNWDIE ETTDIFVHMM PFYSYDIPHT
     CGPEPAICCQ FDFARMRGFS YESCPWRFDP VETNPDNVKE RATKLLDQYR KKSTLYRTNT
     LLVPLGDDFR YVSVEEAEVQ FRNYEKLFDY INSNPHLNAE VKFGTLEDYF STLRDEAEKI
     NYTRPGELGS AELQGFPTLS GDFFTYADRN QDYWSGYYVS RPFFKAVDRV LEQTLRASEI
     LGSFVLGYCQ KFQCAKLPIS FSHKLTAARR NLALFQHHDG VTGTAKDHVV VDYGTRMHTS
     LQDLQLFMSR AVEVLLGDFH DRSDPTLLSH FEPVQERSKY DVQPVHRVLH PDEGKAQSVV
     FFNPLEQTRD EVVMVVVSTP DVSVLNSNGS CLPSQVSPEW QFVSNEKIST GRHRLYWRAS
     VPPLGLETYY VVTGQDCEKA IPAVVKRYTA AQEFPCPEPY HCSKLEGKTV EMKNSNYTLS
     FDTSHGLLQT VTRHKDGEQT VIGEEIGMYR SHGSGAYLFK PVGEARSIVE GGGHFILTEG
     PLVQEAHSLP KTEWHESPLS HSTRMYNCGD SVQDMLIEKE YHVELVGHAF NDKELIVRYK
     TDIDNQRIFY SDLNGFQMSR RQTYDKIPLQ GNYYPMPSLA FLQDSHGKRF SVHSKQSLGA
     ASLKNGWLEI MLDRRLVQDD GRGLGQGVMD NRPMNVIFHL LMESNVSALP KTHSLLTLQP
     SLLSHRVGAH LNYPMHAFMS KKPHGKSFKL AQQSFAPLAA SLPCDVHIVN LKVPQPLRFP
     HTEAAEPRFA VLLQRRGWDA SYCKRGGLQC TTVGEEPVNL FYMFKDLSAV NVKATSLNLL
     HDDPEMLGYL EQIGDVAQEG NVLISPMEIQ AYKLDLQPPS TQEE
//
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