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MAN6_ARATH
ID   MAN6_ARATH              Reviewed;         448 AA.
AC   Q9LZV3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 6;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 6;
DE   AltName: Full=Endo-beta-1,4-mannanase 6;
DE            Short=AtMAN6;
DE   Flags: Precursor;
GN   Name=MAN6; OrderedLocusNames=At5g01930; ORFNames=T20L15.200;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   [5]
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: Ubiquitous. {ECO:0000269|PubMed:16897088}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AL162351; CAB82763.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90411.1; -; Genomic_DNA.
DR   EMBL; BT005831; AAO64766.1; -; mRNA.
DR   EMBL; AK227325; BAE99339.1; -; mRNA.
DR   PIR; T48214; T48214.
DR   RefSeq; NP_195813.1; NM_120271.4.
DR   AlphaFoldDB; Q9LZV3; -.
DR   SMR; Q9LZV3; -.
DR   STRING; 3702.AT5G01930.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; Q9LZV3; -.
DR   PRIDE; Q9LZV3; -.
DR   ProteomicsDB; 238867; -.
DR   DNASU; 831699; -.
DR   EnsemblPlants; AT5G01930.1; AT5G01930.1; AT5G01930.
DR   GeneID; 831699; -.
DR   Gramene; AT5G01930.1; AT5G01930.1; AT5G01930.
DR   KEGG; ath:AT5G01930; -.
DR   Araport; AT5G01930; -.
DR   TAIR; locus:2180987; AT5G01930.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   InParanoid; Q9LZV3; -.
DR   OMA; EMYLGMP; -.
DR   OrthoDB; 1003648at2759; -.
DR   PhylomeDB; Q9LZV3; -.
DR   BioCyc; ARA:AT5G01930-MON; -.
DR   BRENDA; 3.2.1.78; 399.
DR   PRO; PR:Q9LZV3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZV3; baseline and differential.
DR   Genevisible; Q9LZV3; 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   GO; GO:0009845; P:seed germination; 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.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..448
FT                   /note="Mannan endo-1,4-beta-mannosidase 6"
FT                   /id="PRO_0000277479"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
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        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  50622 MW;  977B341312A54D7D CRC64;
     MKDQLGFRIV LCSAVFIILT QNRALADLDS ESHEVNSESV GEEQWEMVQR KGMQFTLNGQ
     PFYVNGFNTY WMMTLAADNS TRGKVTEVFQ QASAVGMTVG RTWAFNDGQW RALQKSPSVY
     DEEVFKALDF VLSEARKYKI RLILSLVNNW DAYGGKAQYV KWGNASGLNL TSDDDFFTNP
     TLRNFYQSHV RTVLNRVNTF TNITYKNDPT IFAWELMNEP RCPSDPSGDK LQSWIQEMAV
     FVKSLDAKHL VEIGLEGFYG PSAPARTRFN PNPYAAQVGT DFIRNNQVLG IDFASVHVYP
     DSWISPAVSN SFLEFTSSWM QAHVEDAEMY LGMPVLFTEF GVSAHDPGFN TSFRDMMLNT
     VYKMTLNSTR KGGAGAGSLV WQVFPQGAEF MDDGYAVYLT RAHTASKIIS LQSKRLAIFN
     SLCSWRCRWG CKKKNQTALD ALLSHDEL
 
 
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