Reviewed, UniProtKB/Swiss-Prot Q8S528 (AL2B7_ARATH)

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase family 2 member B7, mitochondrial
      Short name=ALDH2b
    EC=1.2.1.3

Gene names

Name:	ALDH2B7
Synonyms:	ALDH3
Ordered Locus Names:	At1g23800
ORF Names:	F5O8.33, F5O8.35

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Possesses activity on acetaldehyde and glycolaldehyde in vitro. Ref.1
Catalytic activity	An aldehyde + NAD+ + H2O = an acid + NADH.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion matrix Potential.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Sequence caution	The sequence AAC98035.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAL99612.1 differs from that shown. Reason: Frameshift at positions 303 and 309.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion Potential
	Chain	22 – 534	513	Aldehyde dehydrogenase family 2 member B7, mitochondrial		PRO_0000256057
Regions
	Nucleotide binding	278 – 283	6	NAD By similarity
Sites
	Active site	301	1	Proton acceptor By similarity
	Active site	335	1	Nucleophile By similarity
	Site	202	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8S528-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: C709B0E539E52C31	FASTA	534	58,153
	10 20 30 40 50 60 MASRRVSSLL SRSFMSSSRS IFSLRGMNRG AQRYSNLAAA VENTITPPVK VEHTQLLIGG 70 80 90 100 110 120 RFVDAVSGKT FPTLDPRNGE VIAQVSEGDA EDVNRAVAAA RKAFDEGPWP KMTAYERSKI 130 140 150 160 170 180 LFRFADLIEK HNDEIAALET WDNGKPYEQS AQIEVPMLAR VFRYYAGWAD KIHGMTMPGD 190 200 210 220 230 240 GPHHVQTLHE PIGVAGQIIP WNFPLLMLSW KLGPALACGN TVVLKTAEQT PLSALLVGKL 250 260 270 280 290 300 LHEAGLPDGV VNIVSGFGAT AGAAIASHMD VDKVAFTGST DVGKIILELA SKSNLKAVTL 310 320 330 340 350 360 ELGGKSPFIV CEDADVDQAV ELAHFALFFN QGQCCCAGSR TFVHERVYDE FVEKAKARAL 370 380 390 400 410 420 KRNVGDPFKS GIEQGPQVDS EQFNKILKYI KHGVEAGATL QAGGDRLGSK GYYIQPTVFS 430 440 450 460 470 480 DVKDDMLIAT DEIFGPVQTI LKFKDLDEVI ARANNSRYGL AAGVFTQNLD TAHRLMRALR 490 500 510 520 530 VGTVWINCFD VLDASIPFGG YKMSGIGREK GIYSLNNYLQ VKAVVTSLKN PAWL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the aldehyde dehydrogenase gene families of Zea mays and Arabidopsis." Skibbe D.S., Liu F., Wen T.-J., Yandeau M.D., Cui X., Cao J., Simmons C.R., Schnable P.S. Plant Mol. Biol. 48:751-764(2002) [PubMed: 11999848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF348416 mRNA. Translation: AAL99612.1. Frameshift. AE005172 Genomic DNA. Translation: AAC98035.1. Sequence problems. AY035139 mRNA. Translation: AAK59643.1. AY113912 mRNA. Translation: AAM44960.1.
IPI	IPI00533796.
PIR	C86372.
RefSeq	NP_564204.1.
UniGene	At.22317
3D structure databases
HSSP	HSSP built from PDB template 1O01 based on UniProtKB P05091.
ModBase	Search...
Proteomic databases
PRIDE	Q8S528.
Genome annotation databases
GeneID	838991.
GenomeReviews	Gene locus AT1G23800 in contig CT485782_GR.
KEGG	ath:AT1G23800.
NMPDR	fig|3702.1.peg.2763.
Organism-specific databases
GeneFarm	4318.
TAIR	At1g23800.
Phylogenomic databases
OMA	Q8S528. PFDSQTE.
Enzyme and pathway databases
BRENDA	1.2.1.3. 302.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AL2B7_ARATH

Accession

Primary (citable) accession number: Q8S528
Secondary accession number(s): Q94C67, Q9ZUB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	June 16, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)