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Gamma-aminobutyrate transaminase POP2, mitochondrial (AtGABA-T) (EC 2.6.1.96) (Protein HEXENAL RESPONSE 1) (Protein POLLEN-PISTIL INCOMPATIBILITY 2) (AtPOP2)

 GATP_ARATH              Reviewed;         504 AA.
Q94CE5; B9DHS0; F4J064; Q94FS9; Q9LIE2;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
30-AUG-2017, entry version 118.
RecName: Full=Gamma-aminobutyrate transaminase POP2, mitochondrial {ECO:0000303|Ref.1};
Short=AtGABA-T;
EC=2.6.1.96 {ECO:0000269|PubMed:19264755, ECO:0000269|Ref.1};
AltName: Full=Protein HEXENAL RESPONSE 1;
AltName: Full=Protein POLLEN-PISTIL INCOMPATIBILITY 2;
Short=AtPOP2;
Flags: Precursor;
Name=POP2; Synonyms=GABA-T, HER1; OrderedLocusNames=At3g22200;
ORFNames=MKA23.11;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
AGRICOLA=IND23303939;
Van Cauwenberghe O.R., Makhmoudova A., McLean M.D., Clark S.M.,
Shelp B.J.;
"Plant pyruvate-dependent gamma-aminobutyrate transaminase:
Identification of an Arabidopsis cDNA and its expression in
Escherichia coli.";
Can. J. Bot. 80:933-941(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-504.
STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
LOCATION.
STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
PubMed=12859897; DOI=10.1016/S0092-8674(03)00479-3;
Palanivelu R., Brass L., Edlund A.F., Preuss D.;
"Pollen tube growth and guidance is regulated by POP2, an Arabidopsis
gene that controls GABA levels.";
Cell 114:47-59(2003).
[7]
ENZYME REGULATION.
PubMed=15642352; DOI=10.1016/j.febslet.2004.12.004;
Fait A., Yellin A., Fromm H.;
"GABA shunt deficiencies and accumulation of reactive oxygen
intermediates: insight from Arabidopsis mutants.";
FEBS Lett. 579:415-420(2005).
[8]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18077464; DOI=10.1093/pcp/pcm171;
Miyashita Y., Good A.G.;
"Contribution of the GABA shunt to hypoxia-induced alanine
accumulation in roots of Arabidopsis thaliana.";
Plant Cell Physiol. 49:92-102(2008).
[9]
FUNCTION, AND MUTAGENESIS OF CYS-98 AND GLY-103.
STRAIN=cv. Columbia;
PubMed=17971036; DOI=10.1111/j.1365-313X.2007.03323.x;
Mirabella R., Rauwerda H., Struys E.A., Jakobs C., Triantaphylides C.,
Haring M.A., Schuurink R.C.;
"The Arabidopsis her1 mutant implicates GABA in E-2-hexenal
responsiveness.";
Plant J. 53:197-213(2008).
[10]
MUTAGENESIS OF GLY-271 AND GLY-312, AND DISRUPTION PHENOTYPE.
PubMed=18846220; DOI=10.1371/journal.pone.0003383;
Ludewig F., Hueser A., Fromm H., Beauclair L., Bouche N.;
"Mutants of GABA transaminase (POP2) suppress the severe phenotype of
succinic semialdehyde dehydrogenase (ssadh) mutants in Arabidopsis.";
PLoS ONE 3:E3383-E3383(2008).
[11]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND ENZYME REGULATION.
PubMed=19264755; DOI=10.1093/jxb/erp044;
Clark S.M., Di Leo R., Dhanoa P.K., Van Cauwenberghe O.R.,
Mullen R.T., Shelp B.J.;
"Biochemical characterization, mitochondrial localization, expression,
and potential functions for an Arabidopsis gamma-aminobutyrate
transaminase that utilizes both pyruvate and glyoxylate.";
J. Exp. Bot. 60:1743-1757(2009).
[12]
DISRUPTION PHENOTYPE, AND INDUCTION BY SALT.
PubMed=20122158; DOI=10.1186/1471-2229-10-20;
Renault H., Roussel V., El Amrani A., Arzel M., Renault D.,
Bouchereau A., Deleu C.;
"The Arabidopsis pop2-1 mutant reveals the involvement of GABA
transaminase in salt stress tolerance.";
BMC Plant Biol. 10:20-20(2010).
[13]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=21471118; DOI=10.1093/pcp/pcr041;
Renault H., El Amrani A., Palanivelu R., Updegraff E.P., Yu A.,
Renou J.P., Preuss D., Bouchereau A., Deleu C.;
"GABA accumulation causes cell elongation defects and a decrease in
expression of genes encoding secreted and cell wall-related proteins
in Arabidopsis thaliana.";
Plant Cell Physiol. 52:894-908(2011).
-!- FUNCTION: Transaminase that degrades gamma-amino butyric acid
(GABA) and uses pyruvate or glyoxylate as amino-group acceptor,
but not 2-oxoglutarate. The pyruvate-dependent activity is
reversible while the glyoxylate-dependent activity is
irreversible. Cannot use beta-alanine, ornithine, acetylornithine,
serine, glycine, asparagine, glutamine, glutamate, valine,
leucine, isoleucine, methionine, phenylalanine, histidine, lysine,
arginine, aspartate, threonine, tyrosine, tryptophan, proline, or
cysteine as amino donors. Modulates steady-state GABA levels in
diploid pistil cells and the haploid pollen tube. Involved in the
formation of a gradient of GABA along the pollen tube path.
{ECO:0000269|PubMed:12859897, ECO:0000269|PubMed:17971036,
ECO:0000269|PubMed:19264755, ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY: 4-aminobutanoate + pyruvate = succinate
semialdehyde + L-alanine. {ECO:0000269|PubMed:19264755,
ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY: 4-aminobutanoate + glyoxylate = succinate
semialdehyde + glycine. {ECO:0000269|PubMed:19264755,
ECO:0000269|Ref.1}.
-!- ENZYME REGULATION: Inhibited by gamma-vinyl-gamma-aminobutyrate
(vigabatrin), beta-alanine and ornithine.
{ECO:0000269|PubMed:15642352, ECO:0000269|PubMed:19264755}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.34 mM for GABA (with pyruvate as cosubstrate)
{ECO:0000269|PubMed:19264755};
KM=0.18 mM for GABA (with glyoxylate as cosubstrate)
{ECO:0000269|PubMed:19264755};
KM=0.14 mM for pyruvate (with GABA as cosubstrate)
{ECO:0000269|PubMed:19264755};
KM=0.11 mM for glyoxylate (with GABA as cosubstrate)
{ECO:0000269|PubMed:19264755};
KM=2.4 mM for alanine (with succinic semialdehyde as
cosubstrate) {ECO:0000269|PubMed:19264755};
KM=2.2 mM for alanine (with glyoxylate as cosubstrate)
{ECO:0000269|PubMed:19264755};
KM=0.014 mM for succinic semialdehyde (with alanine as
cosubstrate) {ECO:0000269|PubMed:19264755};
KM=0.14 mM for glyoxylate (with alanine as cosubstrate)
{ECO:0000269|PubMed:19264755};
Vmax=11.9 umol/min/mg enzyme toward GABA in the forward reaction
(with pyruvate as cosubstrate) {ECO:0000269|PubMed:19264755};
Vmax=7.89 umol/min/mg enzyme toward GABA in the forward reaction
(with glyoxylate as cosubstrate) {ECO:0000269|PubMed:19264755};
Vmax=11.9 umol/min/mg enzyme toward pyruvate in the forward
reaction {ECO:0000269|PubMed:19264755};
Vmax=10.9 umol/min/mg enzyme toward glyoxylate in the forward
reaction {ECO:0000269|PubMed:19264755};
Vmax=17.4 umol/min/mg enzyme toward alanine in the reverse
reaction (with succinic semialdehyde as cosubstrate)
{ECO:0000269|PubMed:19264755};
Vmax=15.8 umol/min/mg enzyme toward alanine in the reverse
reaction (with glyoxylate as cosubstrate)
{ECO:0000269|PubMed:19264755};
Vmax=12.1 umol/min/mg enzyme toward succinic semialdehyde in the
reverse reaction {ECO:0000269|PubMed:19264755};
Vmax=13.6 umol/min/mg enzyme toward glyoxylate in the reverse
reaction {ECO:0000269|PubMed:19264755};
pH dependence:
Optimum pH is 9.0 in the forward reaction.
{ECO:0000269|PubMed:19264755};
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12859897,
ECO:0000269|PubMed:19264755}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q94CE5-1; Sequence=Displayed;
Name=2;
IsoId=Q94CE5-2; Sequence=VSP_042907;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems, leaves,
shoots and roots. Detected in reproductive tissues, in the stigma,
style, abscission zone of siliques, stamens and pollen. Not found
in pollen tubes or the transmitting tract. In vegetative tissues,
found in dark-grown hypocotyls, leaves, guard cells and primary
roots, including the root tips and the elongation zones. Not found
in the division zone of the root. {ECO:0000269|PubMed:18077464,
ECO:0000269|PubMed:21471118}.
-!- INDUCTION: Not induced by hypoxia. Up-regulated by salt stress.
{ECO:0000269|PubMed:20122158}.
-!- DISRUPTION PHENOTYPE: No vegetative phenotype. Oversensitivity to
ionic stress but not to osmotic stress. Sustained roots growth
upon treatment with E-2-hexenal. Increased gamma-amino butyric
acid (GABA) in leaves and flowers and defects in pollen tube
growth, guidance and fertility. Cell elongation defects.
{ECO:0000269|PubMed:12859897, ECO:0000269|PubMed:18077464,
ECO:0000269|PubMed:18846220, ECO:0000269|PubMed:20122158,
ECO:0000269|PubMed:21471118}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB03068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF351125; AAK52899.1; -; mRNA.
EMBL; AY034923; AAK59430.1; -; mRNA.
EMBL; AY142571; AAN13140.1; -; mRNA.
EMBL; AP001306; BAB03068.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE76602.1; -; Genomic_DNA.
EMBL; CP002686; AEE76603.1; -; Genomic_DNA.
EMBL; AK317625; BAH20287.1; -; mRNA.
RefSeq; NP_001189947.1; NM_001203018.1. [Q94CE5-2]
RefSeq; NP_566700.1; NM_113117.4. [Q94CE5-1]
UniGene; At.22661; -.
UniGene; At.48693; -.
ProteinModelPortal; Q94CE5; -.
SMR; Q94CE5; -.
BioGrid; 7116; 1.
STRING; 3702.AT3G22200.2; -.
PaxDb; Q94CE5; -.
PRIDE; Q94CE5; -.
EnsemblPlants; AT3G22200.1; AT3G22200.1; AT3G22200. [Q94CE5-1]
EnsemblPlants; AT3G22200.2; AT3G22200.2; AT3G22200. [Q94CE5-2]
GeneID; 821784; -.
Gramene; AT3G22200.1; AT3G22200.1; AT3G22200.
Gramene; AT3G22200.2; AT3G22200.2; AT3G22200.
KEGG; ath:AT3G22200; -.
Araport; AT3G22200; -.
TAIR; locus:2090414; AT3G22200.
eggNOG; ENOG410IR3Y; Eukaryota.
eggNOG; COG0161; LUCA.
HOGENOM; HOG000020207; -.
KO; K16871; -.
OMA; FRIAPPI; -.
PhylomeDB; Q94CE5; -.
BioCyc; MetaCyc:AT3G22200-LER-MONOMER; -.
BRENDA; 2.6.1.19; 399.
BRENDA; 2.6.1.96; 399.
PRO; PR:Q94CE5; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q94CE5; AT.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0003867; F:4-aminobutyrate transaminase activity; IMP:CACAO.
GO; GO:0050897; F:cobalt ion binding; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
GO; GO:0019484; P:beta-alanine catabolic process; IMP:TAIR.
GO; GO:0010154; P:fruit development; IMP:TAIR.
GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:TAIR.
GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:TAIR.
GO; GO:0006540; P:glutamate decarboxylation to succinate; IMP:TAIR.
GO; GO:0006536; P:glutamate metabolic process; IMP:TAIR.
GO; GO:0006541; P:glutamine metabolic process; IMP:TAIR.
GO; GO:0006020; P:inositol metabolic process; IMP:TAIR.
GO; GO:0009865; P:pollen tube adhesion; IMP:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0010033; P:response to organic substance; IMP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
GO; GO:0006105; P:succinate metabolic process; IMP:TAIR.
GO; GO:0005985; P:sucrose metabolic process; IMP:TAIR.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
Alternative splicing; Aminotransferase; Complete proteome;
Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 18 Mitochondrion. {ECO:0000255}.
CHAIN 19 504 Gamma-aminobutyrate transaminase POP2,
mitochondrial.
/FTId=PRO_0000416847.
REGION 158 159 Pyridoxal phosphate binding.
{ECO:0000250}.
BINDING 191 191 Substrate. {ECO:0000250}.
BINDING 298 298 Pyridoxal phosphate. {ECO:0000250}.
BINDING 327 327 Substrate. {ECO:0000250}.
BINDING 458 458 Substrate. {ECO:0000250}.
MOD_RES 327 327 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 1 15 MVVINSLRRLARTTQ -> MPTIVNKNLIFFQNAKLTWIRM
KK (in isoform 2). {ECO:0000305}.
/FTId=VSP_042907.
MUTAGEN 98 98 C->Y: In her1-1; loss of E2-hexenal
responses. {ECO:0000269|PubMed:17971036}.
MUTAGEN 103 103 G->N: In her1-2; loss of E2-hexenal
responses. {ECO:0000269|PubMed:17971036}.
MUTAGEN 271 271 G->E: In pop2-6; Loss of activity and
complete sterility.
{ECO:0000269|PubMed:18846220}.
MUTAGEN 312 312 G->D: In pop2-7; loss of activity.
{ECO:0000269|PubMed:18846220}.
CONFLICT 21 21 K -> R (in Ref. 1; AAK52899).
{ECO:0000305}.
SEQUENCE 504 AA; 55187 MW; BA339283CC72B05F CRC64;
MVVINSLRRL ARTTQVHLHS KYATCMSGNS TSRRIFTTEA APEKKNTVGS KGHDMLAPFT
AGWQSADLDP LVIAKSEGSY VYDDTGKKYL DSLAGLWCTA LGGNEPRLVS AAVEQLNTLP
FYHSFWNRTT KPSLDLAKVL LEMFTANKMA KAFFTSGGSD ANDTQVKLVW YYNNALGRPE
KKKFIARKKS YHGSTLISAS LSGLPPLHQN FDLPAPFVLH TDCPHYWRFH LPGETEEEFS
TRLAKNLEDL IIKEGPETIG AFIAEPVMGA GGVIPPPATY FEKVQAVVKK YDILFIADEV
ICAFGRLGTM FGCDKYNIKP DLVTLAKALS SAYMPIGAIL MSQEVADVIN SHSSKLGVFS
HGFTYSGHPV SCAVAIEALK IYKERNIPEY VAKVAPRFQD GVKAFASGSP IIGETRGTGL
ILGTEFVDNK SPNEPFPPEW GVGAFFGAEC QKHGMLVRVA GDGILMSPPL IISPEEIDEL
ISIYGKALKA TEEKVKELKA QHKK


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