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UniProtKB/Swiss-Prot entry Q9S795


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BADH1_ARATH
Primary accession number Q9S795
Secondary accession number Q56ZQ8
Integrated into Swiss-Prot on July 11, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 58)
Name and origin of the protein
Protein name Betaine aldehyde dehydrogenase 1, chloroplastic [Precursor]
Synonyms BADH
EC 1.2.1.8
Aldehyde dehydrogenase family 10 member A8
Gene name
Name: ALDH10A8
OrderedLocusNames: At1g74920
ORFNames: F9E10.23, F25A4.11
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 390-501.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NOMENCLATURE.
DOI=10.1016/j.tplants.2004.06.004; PubMed=15358267 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
"The ALDH gene superfamily of Arabidopsis.";
Trends Plant Sci. 9:371-377(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC013258; AAG51938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC008263; AAD55284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY093071; AAM13070.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT008872; AAP68311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087395; AAM64944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK220905; BAD94340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H96778; H96778.
RefSeq NP_565094.1; -.
UniGene At.26779
3D structure databases
HSSP P05091; 1O04. [HSSP ENTRY / PDB]
ModBase Q9S795.
Organism-specific databases
TAIR At1g74920; -.
Gene expression databases
ArrayExpress Q9S795; -.
GermOnline AT1G74920; Arabidopsis thaliana.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS Q9S795.
Genome annotation databases
GeneID 843831; -.
GenomeReviews CT485782_GR; AT1G74920.
KEGG ath:AT1G74920; -.
NMPDR fig|3702.1.peg.7008; -.
Other
ProtoNet Q9S795.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Complete proteome; NAD; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     7  7     Chloroplast (Potential). 
CHAIN   8   501  494     Betaine aldehyde dehydrogenase 1, chloroplastic. PRO_0000007179
NP_BIND   238   243  6     NAD (By similarity). 
ACT_SITE   260   260        Proton acceptor (By similarity). 
ACT_SITE   294   294        Nucleophile (By similarity). 
SITE   162   162  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 54432 Da [This is the MW of the unprocessed precursor] CRC64: BA8B03C28C22453B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAIPMPTRQL FIDGEWREPI LKKRIPIVNP ATEEVIGDIP AATTEDVDVA VNAARRALSR 

        70         80         90        100        110        120 
NKGKDWAKAP GAVRAKYLRA IAAKVNERKT DLAKLEALDC GKPLDEAVWD MDDVAGCFEF 

       130        140        150        160        170        180 
YADLAEGLDA KQKAPVSLPM ESFKSYVLKQ PLGVVGLITP WNYPLLMAVW KVAPSLAAGC 

       190        200        210        220        230        240 
TAILKPSELA SVTCLELADI CREVGLPPGV LNVLTGFGSE AGAPLASHPG VDKIAFTGSF 

       250        260        270        280        290        300 
ATGSKVMTAA AQLVKPVSME LGGKSPLIVF DDVDLDKAAE WALFGCFWTN GQICSATSRL 

       310        320        330        340        350        360 
LVHESIASEF IEKLVKWSKN IKISDPMEEG CRLGPVVSKG QYEKILKFIS TAKSEGATIL 

       370        380        390        400        410        420 
HGGSRPEHLE KGFFIEPTII TDVTTSMQIW REEVFGPVLC VKTFASEDEA IELANDSHYG 

       430        440        450        460        470        480 
LGAAVISNDT ERCDRISEAF EAGIVWINCS QPCFTQAPWG GVKRSGFGRE LGEWGLDNYL 

       490        500 
SVKQVTLYTS NDPWGWYKSP N 

Q9S795 in FASTA format

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