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Database: UniProt
Entry: G7KX95_MEDTR
LinkDB: G7KX95_MEDTR
Original site: G7KX95_MEDTR 
ID   G7KX95_MEDTR            Unreviewed;      1061 AA.
AC   G7KX95; A0A0C3WAR8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=11436262 {ECO:0000313|EnsemblPlants:AES80719};
GN   OrderedLocusNames=MTR_7g084030 {ECO:0000313|EMBL:AES80719.2};
GN   ORFNames=MtrunA17_Chr7g0252151 {ECO:0000313|EMBL:RHN47359.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES80719.2, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES80719.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES80719.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES80719,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES80719.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES80719,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES80719}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES80719};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|Proteomes:UP000265566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX   PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA   Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA   Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA   Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA   Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA   Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA   Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 4:1017-1025(2018).
RN   [5] {ECO:0000313|EMBL:RHN47359.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN47359.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(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; CM001223; AES80719.2; -; Genomic_DNA.
DR   EMBL; PSQE01000007; RHN47359.1; -; Genomic_DNA.
DR   RefSeq; XP_003624501.2; XM_003624453.2.
DR   AlphaFoldDB; G7KX95; -.
DR   STRING; 3880.G7KX95; -.
DR   PaxDb; 3880-AES80719; -.
DR   EnsemblPlants; AES80719; AES80719; MTR_7g084030.
DR   GeneID; 11436262; -.
DR   Gramene; AES80719; AES80719; MTR_7g084030.
DR   KEGG; mtr:11436262; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000002051; Chromosome 7.
DR   Proteomes; UP000265566; Chromosome 7.
DR   ExpressionAtlas; G7KX95; differential.
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   CDD; cd10810; GH38N_AMII_LAM_like; 1.
DR   Gene3D; 2.60.40.1360; -; 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; 2.
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   InterPro; IPR048534; Man2a1-like_dom.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF67; 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   Pfam; PF21260; Laman-like_dom; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199, ECO:0000313|EMBL:AES80719.2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          399..473
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1061 AA;  120863 MW;  CF129CC90CD765CD CRC64;
     MITKWKYPSF ILPHRFTKDS IFSNSNVFLF LGCEEFTPLV IFHHPMEKKL IFVVTLLGFL
     FYGGESKFIE YNTSQGVVSG KLNVHLVAHT HDDVGWLKTV DQYYVGSNNS IQGACVQNVL
     DSMVHALLAD KNRKFIYVEI AFFQRWWDDQ SEAVKNIVKQ LVSSGQLEFI NGGMCMHDEA
     VVHYIDMIDQ TTLGHRFLKE EFDLTPRIGW QIDPFGHSAV QAYLLGAEVG FDSLFFGRID
     YQDRNKRKKE KSLEVIWQGS KSLGSSAQIF AGAFPENYEP PSGFYFEVND DSQIVQDNMN
     LFDYNVQDRV NDFVAAALSQ ANITRTNHIM WTMGTDFKYQ YAHTWYRQLD KLIHYVNKDG
     RVNALYSTPS IYTDAKYAAN ESWPIKTDDF FPYSDRANGF WTGYFTSRPA LKRYVRLMSG
     YYLAARQLEY FRGRKKSGPN TDSLADALAI AQHHDAVTGT EKQHVANDYA KRLAIGYKEA
     EELVSSSLAC LVESTSVTGC HNPVIKFQQC PLLNITYCPA SEVELVQGKS LVIVVYNSLG
     WKRNEVIRIP VIDGDVTVHD SKGVEIESQI LPLAEVFVDL RNYYVKAYLG QNPSKTPKYW
     LAFSVSVPPF GFSTYTVSTA KKTGSTRSSV YTLQSHEKSS IGQGNLKLTF STDQQKHTNY
     VNARNMVEEQ VEVSYLYYSG YNGTDQKDPQ NAGAYIFRPN GTHLINHERQ VPVTVLHGPI
     LDEVHQRINP WIYQITRQYK EKEHVEVEFI VGPIPIEDGV GKEVSTRIST TMETNKTFYT
     DSNGRDFIKR VRDYRTDWDL EVHQPVAGNY YPINLGIYVE DDKTEFSVLV DRAIGGSSLG
     DGQIELMLHR RLLLDDSRGV AEALNETDCV ADNCKGLTVQ GKYYYRIDPL GEGAKWRRTF
     GQEIYSPLLL AFSEKDDKDD DWTNTHVTTF SGFDSSYTLP ENIVIITLQE LDHGTVLLRL
     AHLYEIEEDK DLSVVTSVEL KKLFPGKKIK EVKEMSLSAN QERTEMEKKR LVWKVEGSSG
     NEGVSRGGSV DPKERTVELA PMEIRTFTIY FDSSNHLFDA L
//
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