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Protein

Branched-chain-amino-acid aminotransferase 5, chloroplastic

Gene

BCAT5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine (By similarity).By similarity

Catalytic activityi

L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

Cofactori

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-leucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase 2, chloroplastic (IPMS2), 2-isopropylmalate synthase 1, chloroplastic (IPMS1)
  2. 3-isopropylmalate dehydratase small subunit 1 (IPMI2), 3-isopropylmalate dehydratase small subunit 2 (IPMI1), 3-isopropylmalate dehydratase small subunit 3 (At2g43090), 3-isopropylmalate dehydratase large subunit (IIL1)
  3. 3-isopropylmalate dehydrogenase (At1g31180/F28K20_14), 3-isopropylmalate dehydrogenase, 3-isopropylmalate dehydrogenase (IMD1), 3-isopropylmalate dehydrogenase 3, chloroplastic (IMDH3), 3-isopropylmalate dehydrogenase 2, chloroplastic (IMDH2), 3-isopropylmalate dehydrogenase 1, chloroplastic (IMDH1), 3-isopropylmalate dehydrogenase (At5g14200), 3-isopropylmalate dehydrogenase
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase 5, chloroplastic (EC:2.6.1.42)
Short name:
Atbcat-5
Gene namesi
Name:BCAT5
Ordered Locus Names:At5g65780
ORF Names:F6H11.110, MPA24.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G65780.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565ChloroplastSequence analysisAdd
BLAST
Chaini66 – 415350Branched-chain-amino-acid aminotransferase 5, chloroplasticPRO_0000001278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiQ9FYA6.

Expressioni

Gene expression databases

ExpressionAtlasiQ9FYA6. baseline and differential.
GenevisibleiQ9FYA6. AT.

Interactioni

Protein-protein interaction databases

BioGridi21949. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FYA6.
SMRiQ9FYA6. Positions 89-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000276704.
OMAiNCSINDG.
PhylomeDBiQ9FYA6.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FYA6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERSAVASGF HRNYILCASR AATSTTRLHS LSSLRNFPSS SLRIRHCPSP
60 70 80 90 100
ISSNFIVSEV SRNRRCDAVS SSTTDVTELA EIDWDKIDFG LKPTDYMYAM
110 120 130 140 150
KCSRDGEFSQ GQLQPFGNID INPAAGVLNY GQGLFEGLKA YRKQDGNILL
160 170 180 190 200
FRPEENAIRM RNGAERMCMP SPTVEQFVEA VKTTVLANKR WIPPPGKGSL
210 220 230 240 250
YIRPLLMGTG AVLGLAPAPE YTFLIFVSPV GNYFKEGVAP INLIVETEFH
260 270 280 290 300
RATPGGTGGV KTIGNYAAVL KAQSIAKAKG YSDVLYLDCL HKRYLEEVSS
310 320 330 340 350
CNIFIVKDNV ISTPEIKGTI LPGITRKSII EVARSQGFKV EERNVTVDEL
360 370 380 390 400
VEADEVFCTG TAVVLSPVGS ITYKSQRFSY GEDGFGTVSK QLYTSLTSLQ
410
MGLSEDNMNW TVQLS
Length:415
Mass (Da):45,581
Last modified:March 1, 2001 - v1
Checksum:i0E3C6321BDD25247
GO

Sequence cautioni

The sequence BAB10685.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA16682.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At5g65780 and At5g65770.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293804 mRNA. Translation: CAC03680.1.
AB010075 Genomic DNA. Translation: BAB10685.1. Sequence problems.
AL021684 Genomic DNA. Translation: CAA16682.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED98106.1.
RefSeqiNP_201379.2. NM_125975.7. [Q9FYA6-1]
UniGeneiAt.23243.

Genome annotation databases

EnsemblPlantsiAT5G65780.1; AT5G65780.1; AT5G65780. [Q9FYA6-1]
GeneIDi836707.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293804 mRNA. Translation: CAC03680.1.
AB010075 Genomic DNA. Translation: BAB10685.1. Sequence problems.
AL021684 Genomic DNA. Translation: CAA16682.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED98106.1.
RefSeqiNP_201379.2. NM_125975.7. [Q9FYA6-1]
UniGeneiAt.23243.

3D structure databases

ProteinModelPortaliQ9FYA6.
SMRiQ9FYA6. Positions 89-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21949. 1 interaction.

Proteomic databases

PRIDEiQ9FYA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G65780.1; AT5G65780.1; AT5G65780. [Q9FYA6-1]
GeneIDi836707.

Organism-specific databases

TAIRiAT5G65780.

Phylogenomic databases

HOGENOMiHOG000276704.
OMAiNCSINDG.
PhylomeDBiQ9FYA6.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Miscellaneous databases

PROiQ9FYA6.

Gene expression databases

ExpressionAtlasiQ9FYA6. baseline and differential.
GenevisibleiQ9FYA6. AT.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins."
    Diebold R., Schuster J., Daschner K., Binder S.
    Plant Physiol. 129:540-550(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiBCAT5_ARATH
AccessioniPrimary (citable) accession number: Q9FYA6
Secondary accession number(s): O49539, Q9FLG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Branched-chain amino acids are synthesized in chloroplasts, whereas the degradation takes place in mitochondria.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.