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BAM9_ARATH
ID   BAM9_ARATH              Reviewed;         536 AA.
AC   Q8VYW2; Q946D4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Inactive beta-amylase 9;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE   AltName: Full=Inactive beta-amylase 3;
GN   Name=BAM9; Synonyms=BMY3; OrderedLocusNames=At5g18670; ORFNames=T1A4.50;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   DOI=10.1016/S0168-9452(01)00508-8;
RA   Chandler J.W., Apel K., Melzer S.;
RT   "A novel putative beta-amylase gene and ATbeta-Amy from Arabidopsis
RT   thaliana are circadian regulated.";
RL   Plant Sci. 161:1019-1024(2001).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18390594; DOI=10.1105/tpc.107.056507;
RA   Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P.,
RA   Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K.,
RA   Smith A.M., Smith S.M., Zeeman S.C.;
RT   "Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts
RT   upstream of three active beta-amylases in Arabidopsis chloroplasts.";
RL   Plant Cell 20:1040-1058(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in young floral buds, flowers and
CC       roots, and, to a later extent, in stems and leaves.
CC       {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: Circadian-regulated, with a peak in expression just before
CC       the light period in short day conditions. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the family, lacks the
CC       conserved Glu active site in position 449, which is replaced by a Gln
CC       residue, suggesting it is inactive. {ECO:0000305}.
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DR   EMBL; AF402598; AAK85300.1; -; mRNA.
DR   EMBL; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92597.1; -; Genomic_DNA.
DR   EMBL; AY069879; AAL47434.1; -; mRNA.
DR   EMBL; AY142007; AAM98271.1; -; mRNA.
DR   EMBL; AY087036; AAM64597.1; -; mRNA.
DR   RefSeq; NP_197368.1; NM_121872.3.
DR   AlphaFoldDB; Q8VYW2; -.
DR   SMR; Q8VYW2; -.
DR   STRING; 3702.AT5G18670.1; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   PaxDb; Q8VYW2; -.
DR   PRIDE; Q8VYW2; -.
DR   ProteomicsDB; 240708; -.
DR   EnsemblPlants; AT5G18670.1; AT5G18670.1; AT5G18670.
DR   GeneID; 831985; -.
DR   Gramene; AT5G18670.1; AT5G18670.1; AT5G18670.
DR   KEGG; ath:AT5G18670; -.
DR   Araport; AT5G18670; -.
DR   TAIR; locus:2180029; AT5G18670.
DR   eggNOG; ENOG502QPTU; Eukaryota.
DR   HOGENOM; CLU_016754_5_0_1; -.
DR   InParanoid; Q8VYW2; -.
DR   OMA; RFSWAGY; -.
DR   OrthoDB; 533202at2759; -.
DR   PhylomeDB; Q8VYW2; -.
DR   PRO; PR:Q8VYW2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8VYW2; baseline and differential.
DR   Genevisible; Q8VYW2; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016161; F:beta-amylase activity; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; PTHR31352; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Phosphoprotein;
KW   Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..536
FT                   /note="Inactive beta-amylase 9"
FT                   /id="PRO_0000393423"
FT   REGION          511..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LIR6"
FT   CONFLICT        69..70
FT                   /note="DD -> GA (in Ref. 1; AAK85300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442..443
FT                   /note="QG -> RKA (in Ref. 1; AAK85300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   536 AA;  58281 MW;  C21F0582BE72E190 CRC64;
     MEVSVIGNPQ ARICRAELAY RELGFRFGSD VISGESRNRV SFCNQSSKWK EIAIRCSSRS
     VKCEAIVSDD ASPFLKSTPK SKSLESVKLF VGLPLDTVSD CNNVNHLKAI TAGLKALKLL
     GVEGIELPIF WGVVEKEAAG KYEWSGYLAV AEIVKKVGLK LHASLSFHGS KQTEIGLPDW
     VAKIGDAEPG IYFTDRYGQQ YKDCLSFAVD DVPVLDGKTP MEVYRGFCES FKSAFADYMG
     NTITGITLGL GPDGELKYPS HQHNAKLSGA GEFQCYDKHM LSALKGYAES TGNPLWGLGG
     PHDAPAYDQQ PNSSSFFSDG GSWESQYGDF FLSWYSSLLT SHADRVLSVA SSAFSGIGVP
     LCGKLPLLHQ WHKLRSHPSE LTAGFYSSNG QDRYEAIAEI FAKNSCRMII PGMDLSDEHQ
     SPESLSSPES LLGHIKTSCK KQGVVVSGQN SSTPVPGGFE RIVENLKDEN VGIDLFTYQR
     MGALFFSPEH FHAFTVFVRN LSQFELSSDD QASEAEVEAE TASIGSGTGA PSLQTA
 
 
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