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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