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MAN1_ARATH
ID   MAN1_ARATH              Reviewed;         411 AA.
AC   Q9FZ29;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 1;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 1;
DE   AltName: Full=Endo-beta-1,4-mannanase 1;
DE            Short=AtMAN1;
DE   Flags: Precursor;
GN   Name=MAN1; OrderedLocusNames=At1g02310; ORFNames=T6A9.1;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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 roots, stems and flowers.
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; AC064879; AAG00883.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27414.1; -; Genomic_DNA.
DR   EMBL; AY081352; AAL91241.1; -; mRNA.
DR   EMBL; BT002154; AAN72165.1; -; mRNA.
DR   PIR; D86153; D86153.
DR   RefSeq; NP_171733.2; NM_100112.3.
DR   AlphaFoldDB; Q9FZ29; -.
DR   SMR; Q9FZ29; -.
DR   STRING; 3702.AT1G02310.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; Q9FZ29; -.
DR   PRIDE; Q9FZ29; -.
DR   ProteomicsDB; 238552; -.
DR   EnsemblPlants; AT1G02310.1; AT1G02310.1; AT1G02310.
DR   GeneID; 839444; -.
DR   Gramene; AT1G02310.1; AT1G02310.1; AT1G02310.
DR   KEGG; ath:AT1G02310; -.
DR   Araport; AT1G02310; -.
DR   TAIR; locus:2204878; AT1G02310.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   InParanoid; Q9FZ29; -.
DR   PhylomeDB; Q9FZ29; -.
DR   PRO; PR:Q9FZ29; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FZ29; baseline and differential.
DR   Genevisible; Q9FZ29; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..411
FT                   /note="Mannan endo-1,4-beta-mannosidase 1"
FT                   /id="PRO_0000277474"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  46290 MW;  B72ECB54C4D7F218 CRC64;
     MLNILPFFLF FLPFLIGNNR ICVAVKTGFV GRNGTQFVLN GEQVYLNGFN AYWMMTTAAD
     TASKGRATVT TALRQASAVG MNVARIWGFN EGDYIPLQIS PGSYSEDVFK GLDFVVYEAG
     RFNIKLIISL VNNFEDYGGR KKYVEWAGLD EPDEFYTNSA VKQFYKNHVK TVLTRKNTIT
     GRMYKDDPTI FSWELINEPR CNDSTASNIL QDWVKEMASY VKSIDSNHLL EIGLEGFYGE
     SIPERTVYNP GGRVLTGTDF ITNNQIPDID FATIHIYPDS WLPLQSSRTG EQDTFVDRWI
     GAHIEDCDNI IKKPLLITEF GKSSKYPGFS LEKRNKFFQR VYDVIYDSAR AGGSCTGGVF
     WQLTTNRTGL LGDGYEVFMQ AGPNTTAQLI ADQSSKLKNL KYPPLVTHSA E
 
 
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