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MAN3_ARATH
ID   MAN3_ARATH              Reviewed;         414 AA.
AC   Q9SG94;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 3;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 3;
DE   AltName: Full=Endo-beta-1,4-mannanase 3;
DE            Short=AtMAN3;
DE   Flags: Precursor;
GN   Name=MAN3; OrderedLocusNames=At3g10890; ORFNames=T7M13.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND TISSUE SPECIFICITY.
RX   PubMed=16897088; DOI=10.1007/s10142-006-0034-3;
RA   Yuan J.S., Yang X., Lai J., Lin H., Cheng Z.-M., Nonogaki H., Chen F.;
RT   "The endo-beta-mannanase gene families in Arabidopsis, rice, and poplar.";
RL   Funct. Integr. Genomics 7:1-16(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC         mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, siliques and seeds.
CC       {ECO:0000269|PubMed:16897088}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AC011708; AAF19560.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74967.1; -; Genomic_DNA.
DR   RefSeq; NP_187700.1; NM_111926.2.
DR   AlphaFoldDB; Q9SG94; -.
DR   SMR; Q9SG94; -.
DR   STRING; 3702.AT3G10890.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; Q9SG94; -.
DR   PRIDE; Q9SG94; -.
DR   ProteomicsDB; 238234; -.
DR   EnsemblPlants; AT3G10890.1; AT3G10890.1; AT3G10890.
DR   GeneID; 820259; -.
DR   Gramene; AT3G10890.1; AT3G10890.1; AT3G10890.
DR   KEGG; ath:AT3G10890; -.
DR   Araport; AT3G10890; -.
DR   TAIR; locus:2103262; AT3G10890.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   InParanoid; Q9SG94; -.
DR   OMA; HVKTMVN; -.
DR   OrthoDB; 1003648at2759; -.
DR   PhylomeDB; Q9SG94; -.
DR   BioCyc; ARA:AT3G10890-MON; -.
DR   PRO; PR:Q9SG94; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SG94; baseline and differential.
DR   Genevisible; Q9SG94; AT.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:TAIR.
DR   GO; GO:0071585; P:detoxification of cadmium ion; IMP:TAIR.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045053; MAN-like.
DR   PANTHER; PTHR31451; PTHR31451; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..414
FT                   /note="Mannan endo-1,4-beta-mannosidase 3"
FT                   /id="PRO_0000277476"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        323
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  46462 MW;  BBACD11830EB2609 CRC64;
     MKCLCFVVLL AILIAQNSSD LGVKSASSDG FVSRKGVQFI LNGKPFYANG FNAYWLAYEA
     TDSTTRFKIT YVFQNATIHD LTIVRTWGFR DGGYRALQIA PGVYDEKTFQ GLDFAIAEAK
     RLGIKMIITF VNNYSDFGGR KQYVDWAKNT GQNVSSDDDF YTNPLVKQYY KNHVKTMVNR
     VNTFTKVEYK DEPTIMGWEL MNEPQCRADP SGKTLTAWMN EMALYVKSVD SKHLLSTGLE
     GFYGDSSPQR KTSLNPVAAN VLGTDFIANH KLDAIDFASI HSYPDLWFPN LDEKSRLNLL
     RKWLECHLED AQNILKKPLI LGEFGKPTNT PGYTQAQRDA VFNATFDTIY ESAEKGGPAA
     GALFWHVISD GMNNFKDPLS IVLSENSTTV NIITEESRKL GLIRGKGKLS KTKI
 
 
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