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UniProtKB/Swiss-Prot entry Q8VZC3


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

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Entry information
Entry name AL121_ARATH
Primary accession number Q8VZC3
Secondary accession numbers Q93Y55 Q9FJJ2
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 46)
Name and origin of the protein
Protein name Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial [Precursor]
Synonyms P5C dehydrogenase
AtP5CDH
EC 1.5.1.12
Aldehyde dehydrogenase family 12 member A1
Gene name
Name: ALDH12A1
Synonyms: P5CDH
OrderedLocusNames: At5g62530
ORFNames: K19B1.14
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11532180 [NCBI, ExPASy, EBI, Israel, Japan]
Deuschle K., Funck D., Hellmann H., Daeschner K., Binder S., Frommer W.B.;
"A nuclear gene encoding mitochondrial delta-1-pyrroline-5-carboxylate dehydrogenase and its potential role in protection from proline toxicity.";
Plant J. 27:345-356(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/5.5.297; PubMed=9872454 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones.";
DNA Res. 5:297-308(1998).
[3]
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).
[4]
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
AY039787; AAK73756.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015469; BAB11503.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065072; AAL38248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000746; AAN31887.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT010391; AAQ56834.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_568955.1; -.
UniGene At.9309
3D structure databases
ModBase Q8VZC3.
Organism-specific databases
GeneFarm 4315; -.
TAIR At5g62530; -.
Gene expression databases
ArrayExpress Q8VZC3; -.
GermOnline AT5G62530; Arabidopsis thaliana.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from TAIR).
GO:0003842; Molecular function: 1-pyrroline-5-carboxylate dehydrogenase activity (inferred from mutant phenotype from TAIR).
GO:0010133; Biological process: proline catabolic process to glutamate (inferred from mutant phenotype from TAIR).
QuickGo view.
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; FALSE_NEG.
BLOCKS Q8VZC3.
Genome annotation databases
GeneID 836373; -.
GenomeReviews BA000015_GR; AT5G62530.
KEGG ath:AT5G62530; -.
NMPDR fig|3702.1.peg.28292; -.
Other
ProtoNet Q8VZC3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   556        Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial. PRO_0000256062
NP_BIND   282   287  6     NAD (By similarity). 
ACT_SITE   301   301        Proton acceptor (By similarity). 
ACT_SITE   336   336        Nucleophile (By similarity). 
SITE   207   207  1     Transition state stabilizer (By similarity). 
CONFLICT   48    48        A -> S (in Ref. 1; AAK73756). 
CONFLICT   462   462        E -> D (in Ref. 1; AAK73756). 
Sequence information
Length: 556 AA [This is the length of the unprocessed precursor] Molecular weight: 61773 Da [This is the MW of the unprocessed precursor] CRC64: 83F19E7A300D5565 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MYRVFASRAL RAKSLCDKSS TSLASLTLSR LNHSIPFATV DAEELSGAHP AEVQSFVQGK 

        70         80         90        100        110        120 
WIGSSNHNTL LDPLNGEPFI KVAEVDESGT QPFVDSLSQC PKHGLHNPFK SPERYLLYGD 

       130        140        150        160        170        180 
ISTKAAHMLA LPKVADFFAR LIQRVAPKSY QQAAGEVFVT RKFLENFCGD QVRFLARSFA 

       190        200        210        220        230        240 
IPGNHLGQQS HGYRWPYGPV TIVTPFNFPL EIPLLQLMGA LYMGNKPLLK VDSKVSIVME 

       250        260        270        280        290        300 
QMMRLLHYCG LPAEDVDFIN SDGKTMNKIL LEANPRMTLF TGSSRVAEKL ALDLKGRIRL 

       310        320        330        340        350        360 
EDAGFDWKVL GPDVQEVDYV AWQCDQDAYA CSGQKCSAQS MLFVHENWSK TPLVSKLKEL 

       370        380        390        400        410        420 
AERRKLEDLT IGPVLTFTTE AMLEHMENLL QIPGSKLLFG GKELKNHSIP SIYGALEPTA 

       430        440        450        460        470        480 
VYVPIEEILK DNKTYELVTK EIFGPFQIVT EYKKDQLPLV LEALERMHAH LTAAVVSNDP 

       490        500        510        520        530        540 
IFLQEVIGNS VNGTTYAGLR GRTTGAPQNH WFGPAGDPRG AGIGTPEAIK LVWSCHREVI 

       550 
YDYGPVPQGW ELPPST 

Q8VZC3 in FASTA format

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