ID   MAN5_ARATH              Reviewed;         431 AA.
AC   Q9M0H6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 5;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 5;
DE   AltName: Full=Endo-beta-1,4-mannanase 5;
DE            Short=AtMAN5;
DE   Flags: Precursor;
GN   Name=MAN5; OrderedLocusNames=At4g28320; ORFNames=F26K10.200;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
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: Expressed in stems. {ECO:0000269|PubMed:16897088}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AL161572; CAB79634.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85469.1; -; Genomic_DNA.
DR   EMBL; AK228732; BAF00634.1; -; mRNA.
DR   EMBL; BT026124; ABG48480.1; -; mRNA.
DR   PIR; T09048; T09048.
DR   RefSeq; NP_194561.1; NM_118972.5.
DR   AlphaFoldDB; Q9M0H6; -.
DR   SMR; Q9M0H6; -.
DR   STRING; 3702.Q9M0H6; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GlyCosmos; Q9M0H6; 4 sites, No reported glycans.
DR   iPTMnet; Q9M0H6; -.
DR   PaxDb; 3702-AT4G28320-1; -.
DR   ProteomicsDB; 238651; -.
DR   EnsemblPlants; AT4G28320.1; AT4G28320.1; AT4G28320.
DR   GeneID; 828947; -.
DR   Gramene; AT4G28320.1; AT4G28320.1; AT4G28320.
DR   KEGG; ath:AT4G28320; -.
DR   Araport; AT4G28320; -.
DR   TAIR; AT4G28320; MAN5.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   InParanoid; Q9M0H6; -.
DR   OMA; LFWQYGQ; -.
DR   OrthoDB; 2717493at2759; -.
DR   PhylomeDB; Q9M0H6; -.
DR   BioCyc; ARA:AT4G28320-MONOMER; -.
DR   BRENDA; 3.2.1.78; 399.
DR   PRO; PR:Q9M0H6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0H6; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045053; MAN-like.
DR   PANTHER; PTHR31451:SF48; MANNAN ENDO-1,4-BETA-MANNOSIDASE 5; 1.
DR   PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   Genevisible; Q9M0H6; AT.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..431
FT                   /note="Mannan endo-1,4-beta-mannosidase 5"
FT                   /id="PRO_0000277478"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  49899 MW;  3EEDCC0BE61EC90A CRC64;
     MVPTRNRPML RILGFFICAA FIYLSFRDLW LNHKGKAKLG FVKRNGTQFV VDDKPLYVNG
     WNSYWFMDHA VDEHSRNLVG EMLEAGAKMG LTVCRTWAFN DGGYNALQIS PGRFDERVFQ
     ALDHVIAEAR KHDVRLLLSL VNNLQAYGGK TQYVKWAWQE GVGLSSSNDS FFFDPSIRNY
     FKNYLKVLLT RKNSVTGIEY RNDPTIFAWE LINEPRCTTD VSGKTLQDWI DEMTGFIKSI
     DDKHLLTVGL EGFYGPNSPK GLTVNPEQWA SQLGTDFVQN SNSSNIDFAS VHIYPDHWFH
     NQTFEEKLKF VVKWMQSHIE DGLKELKKPV LFTEFGLSNQ NKDYEPSQRD KFYRIIFDVV
     YKSAKRKKSG AGTLVWQLFM EGMETFNDDF GIVPHEQDSI YKLMIEQSCR LGKVTGRLKE
     QKLKELCSHR H
//