ID   MAN2_ORYSJ              Reviewed;         445 AA.
AC   Q0JJD4; A0A0N7KDR1; Q94J47;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
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   AltName: Full=OsMAN2;
DE   Flags: Precursor;
GN   Name=MAN2; OrderedLocusNames=Os01g0746700, LOC_Os01g54300;
GN   ORFNames=OSJNBa0014K08.42, P0481E12.1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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 and seeds, and at lower levels
CC       in roots and leaves. {ECO:0000269|PubMed:16897088}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP003076; BAB56016.1; -; Genomic_DNA.
DR   EMBL; AP003376; BAC05600.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF06144.2; -; Genomic_DNA.
DR   EMBL; AP014957; BAS74321.1; -; Genomic_DNA.
DR   RefSeq; XP_015626424.1; XM_015770938.1.
DR   AlphaFoldDB; Q0JJD4; -.
DR   SMR; Q0JJD4; -.
DR   STRING; 4530.OS01T0746700-00; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; Q0JJD4; -.
DR   PRIDE; Q0JJD4; -.
DR   EnsemblPlants; Os01t0746700-00; Os01t0746700-00; Os01g0746700.
DR   GeneID; 4326178; -.
DR   Gramene; Os01t0746700-00; Os01t0746700-00; Os01g0746700.
DR   KEGG; osa:4326178; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   InParanoid; Q0JJD4; -.
DR   OMA; QRWMEEM; -.
DR   OrthoDB; 1003648at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q0JJD4; OS.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
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; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..445
FT                   /note="Mannan endo-1,4-beta-mannosidase 2"
FT                   /id="PRO_0000277483"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  50063 MW;  C7A62692B7597FC9 CRC64;
     MAVGNGLILY HILGLASCIA LVYFSLGEVD LRDALPSLPF SGGASRAAAA SLPFVERRGK
     RLFLDGRPFY INGWNSYWLM DLAVEPNTRP RVSSMFRTAV SMGLTVCRTW AFNDGSYNAL
     QLSPGHFDER VFKALDRVVA EASEHGVRLI LSLANNLDAY GGKRQYVRWA WEEGVGLTAS
     NDSFFFDPAI RDYFKVYLKT LLMRKNHLTG LEYRDDPTIL AWELMNEPRC TSDPSGDTLQ
     RWMEEMSAYV KSIDKKHLLT VGTEGFYGPT SSQEKLNINP GEWFPNNYGA DFIRNSKIQD
     IDFASVHVYP DNWLQHASLD EKLKFMTRWI TAHVEDGDGE LEKPVLVTEF GLSHQVEGFE
     DAHRDVLYRA VYDIVHGSAR RGGAAGGALV WQLAAEGMEE YHDGFSIVPS ERPSMMRLIK
     EQSCRLAAVR YGEEGARKVL KTVCA