MAN2_ARATH
ID MAN2_ARATH Reviewed; 433 AA.
AC Q7Y223; Q9SKU9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase 2;
DE EC=3.2.1.78;
DE AltName: Full=Beta-mannanase 2;
DE AltName: Full=Endo-beta-1,4-mannanase 2;
DE Short=AtMAN2;
DE Flags: Precursor;
GN Name=MAN2; OrderedLocusNames=At2g20680; ORFNames=F5H14.35;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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, leaves and seeds.
CC {ECO:0000269|PubMed:16897088}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006234; AAD20927.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07056.1; -; Genomic_DNA.
DR EMBL; BT008596; AAP40422.1; -; mRNA.
DR EMBL; BT025988; ABG25077.1; -; mRNA.
DR EMBL; AK228569; BAF00487.1; -; mRNA.
DR PIR; A84592; A84592.
DR RefSeq; NP_179660.2; NM_127632.3.
DR AlphaFoldDB; Q7Y223; -.
DR SMR; Q7Y223; -.
DR STRING; 3702.AT2G20680.1; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; Q7Y223; -.
DR PRIDE; Q7Y223; -.
DR ProteomicsDB; 238650; -.
DR EnsemblPlants; AT2G20680.1; AT2G20680.1; AT2G20680.
DR GeneID; 816596; -.
DR Gramene; AT2G20680.1; AT2G20680.1; AT2G20680.
DR KEGG; ath:AT2G20680; -.
DR Araport; AT2G20680; -.
DR TAIR; locus:2051399; AT2G20680.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_0_0_1; -.
DR InParanoid; Q7Y223; -.
DR OMA; QRWMEEM; -.
DR OrthoDB; 1003648at2759; -.
DR PhylomeDB; Q7Y223; -.
DR BioCyc; ARA:AT2G20680-MON; -.
DR PRO; PR:Q7Y223; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7Y223; baseline and differential.
DR Genevisible; Q7Y223; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:TAIR.
DR GO; GO:0010412; P:mannan metabolic process; IDA: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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..433
FT /note="Mannan endo-1,4-beta-mannosidase 2"
FT /id="PRO_0000277475"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 49558 MW; DBC5FEBE6749B2D3 CRC64;
MAAPTGNGPV IPILGFLTCV AFIYLSFGDL WFGLKTEGEL AFVKRNGTQF VVDGKALYVN
GWNSYWFMDH AVNDHSRHRV SAMLEAGAKM GLTVCRTWAF NDGGYNALQI SPGRFDERVF
KALDHVIAEA KTHGVRLLLS LVNNLQAYGG KTQYVNWAWQ EGVGLSSSND SFFFDPSIRR
YFKNYLTVLL TRKNSLTGIE YRNDPTIFAW ELINEPRCMS DVSGDTLQDW INEMTAFIKS
IDNKHLLTVG LEGFYGPSSP KKLTVNPERW ASELGSDFVR NSDSPNIDFA SVHIYPDHWF
HDQGFEEKLK FVVKWMLSHI EDGDKELKKP VLFTEFGLSN LNKDYDPSQR DRFYRTIFDV
IYKSAKRKRS GAGTLVWQFL IEGMEGFNDD FGIVPWEQDS IQRLMIEQSC RLSRITGRHL
LDKKSIEMCS HRP
