GATP_ARATH
ID GATP_ARATH Reviewed; 504 AA.
AC Q94CE5; B9DHS0; F4J064; Q94FS9; Q9LIE2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Gamma-aminobutyrate transaminase POP2, mitochondrial {ECO:0000303|PubMed:12859897};
DE Short=AtGABA-T {ECO:0000303|Ref.1};
DE EC=2.6.1.96 {ECO:0000269|PubMed:19264755, ECO:0000269|Ref.1};
DE AltName: Full=Gamma-aminobutyric acid aminotransferase 1 {ECO:0000303|PubMed:21690177};
DE AltName: Full=Protein HEXENAL RESPONSE 1 {ECO:0000303|PubMed:17971036};
DE AltName: Full=Protein POLLEN-PISTIL INCOMPATIBILITY 2 {ECO:0000303|PubMed:12859897};
DE Short=AtPOP2 {ECO:0000303|PubMed:12859897};
DE Flags: Precursor;
GN Name=POP2 {ECO:0000303|PubMed:12859897};
GN Synonyms=GABA-T {ECO:0000303|Ref.1}, GABAT1 {ECO:0000303|PubMed:21690177},
GN HER1 {ECO:0000303|PubMed:17971036};
GN OrderedLocusNames=At3g22200 {ECO:0000312|Araport:AT3G22200};
GN ORFNames=MKA23.11 {ECO:0000312|EMBL:BAB03068.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX AGRICOLA=IND23303939; DOI=10.1139/b02-087;
RA Van Cauwenberghe O.R., Makhmoudova A., McLean M.D., Clark S.M., Shelp B.J.;
RT "Plant pyruvate-dependent gamma-aminobutyrate transaminase: Identification
RT of an Arabidopsis cDNA and its expression in Escherichia coli.";
RL Can. J. Bot. 80:933-941(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-504.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=12859897; DOI=10.1016/s0092-8674(03)00479-3;
RA Palanivelu R., Brass L., Edlund A.F., Preuss D.;
RT "Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene
RT that controls GABA levels.";
RL Cell 114:47-59(2003).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=15642352; DOI=10.1016/j.febslet.2004.12.004;
RA Fait A., Yellin A., Fromm H.;
RT "GABA shunt deficiencies and accumulation of reactive oxygen intermediates:
RT insight from Arabidopsis mutants.";
RL FEBS Lett. 579:415-420(2005).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18077464; DOI=10.1093/pcp/pcm171;
RA Miyashita Y., Good A.G.;
RT "Contribution of the GABA shunt to hypoxia-induced alanine accumulation in
RT roots of Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:92-102(2008).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF CYS-98 AND GLY-103.
RC STRAIN=cv. Columbia;
RX PubMed=17971036; DOI=10.1111/j.1365-313x.2007.03323.x;
RA Mirabella R., Rauwerda H., Struys E.A., Jakobs C., Triantaphylides C.,
RA Haring M.A., Schuurink R.C.;
RT "The Arabidopsis her1 mutant implicates GABA in E-2-hexenal
RT responsiveness.";
RL Plant J. 53:197-213(2008).
RN [10]
RP MUTAGENESIS OF GLY-271 AND GLY-312, AND DISRUPTION PHENOTYPE.
RX PubMed=18846220; DOI=10.1371/journal.pone.0003383;
RA Ludewig F., Hueser A., Fromm H., Beauclair L., Bouche N.;
RT "Mutants of GABA transaminase (POP2) suppress the severe phenotype of
RT succinic semialdehyde dehydrogenase (ssadh) mutants in Arabidopsis.";
RL PLoS ONE 3:E3383-E3383(2008).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=19264755; DOI=10.1093/jxb/erp044;
RA Clark S.M., Di Leo R., Dhanoa P.K., Van Cauwenberghe O.R., Mullen R.T.,
RA Shelp B.J.;
RT "Biochemical characterization, mitochondrial localization, expression, and
RT potential functions for an Arabidopsis gamma-aminobutyrate transaminase
RT that utilizes both pyruvate and glyoxylate.";
RL J. Exp. Bot. 60:1743-1757(2009).
RN [12]
RP DISRUPTION PHENOTYPE, AND INDUCTION BY SALT.
RX PubMed=20122158; DOI=10.1186/1471-2229-10-20;
RA Renault H., Roussel V., El Amrani A., Arzel M., Renault D., Bouchereau A.,
RA Deleu C.;
RT "The Arabidopsis pop2-1 mutant reveals the involvement of GABA transaminase
RT in salt stress tolerance.";
RL BMC Plant Biol. 10:20-20(2010).
RN [13]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21471118; DOI=10.1093/pcp/pcr041;
RA Renault H., El Amrani A., Palanivelu R., Updegraff E.P., Yu A., Renou J.P.,
RA Preuss D., Bouchereau A., Deleu C.;
RT "GABA accumulation causes cell elongation defects and a decrease in
RT expression of genes encoding secreted and cell wall-related proteins in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 52:894-908(2011).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=21690177; DOI=10.1093/pcp/pcr079;
RA Toyokura K., Watanabe K., Oiwaka A., Kusano M., Tameshige T., Tatematsu K.,
RA Matsumoto N., Tsugeki R., Saito K., Okada K.;
RT "Succinic semialdehyde dehydrogenase is involved in the robust patterning
RT of Arabidopsis leaves along the adaxial-abaxial axis.";
RL Plant Cell Physiol. 52:1340-1353(2011).
CC -!- FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA)
CC and uses pyruvate or glyoxylate as amino-group acceptor, but not 2-
CC oxoglutarate. The pyruvate-dependent activity is reversible while the
CC glyoxylate-dependent activity is irreversible. Cannot use beta-alanine,
CC ornithine, acetylornithine, serine, glycine, asparagine, glutamine,
CC glutamate, valine, leucine, isoleucine, methionine, phenylalanine,
CC histidine, lysine, arginine, aspartate, threonine, tyrosine,
CC tryptophan, proline, or cysteine as amino donors. Modulates steady-
CC state GABA levels in diploid pistil cells and the haploid pollen tube.
CC Involved in the formation of a gradient of GABA along the pollen tube
CC path. Involved in the maintenance of the shoot apical meristem (SAM)
CC structure and subsequent adaxial-abaxial axis-dependent development of
CC cotyledons and leaves (PubMed:21690177). {ECO:0000269|PubMed:12859897,
CC ECO:0000269|PubMed:17971036, ECO:0000269|PubMed:19264755,
CC ECO:0000269|PubMed:21690177, ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + pyruvate = L-alanine + succinate
CC semialdehyde; Xref=Rhea:RHEA:32263, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57972, ChEBI:CHEBI:59888; EC=2.6.1.96;
CC Evidence={ECO:0000269|PubMed:19264755, ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + glyoxylate = glycine + succinate
CC semialdehyde; Xref=Rhea:RHEA:32267, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.96;
CC Evidence={ECO:0000269|PubMed:19264755, ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Inhibited by gamma-vinyl-gamma-aminobutyrate
CC (vigabatrin), beta-alanine and ornithine. {ECO:0000269|PubMed:15642352,
CC ECO:0000269|PubMed:19264755}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for GABA (with pyruvate as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=0.18 mM for GABA (with glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=0.14 mM for pyruvate (with GABA as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=0.11 mM for glyoxylate (with GABA as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=2.4 mM for alanine (with succinic semialdehyde as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=2.2 mM for alanine (with glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=0.014 mM for succinic semialdehyde (with alanine as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC KM=0.14 mM for glyoxylate (with alanine as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC Vmax=11.9 umol/min/mg enzyme toward GABA in the forward reaction
CC (with pyruvate as cosubstrate) {ECO:0000269|PubMed:19264755};
CC Vmax=7.89 umol/min/mg enzyme toward GABA in the forward reaction
CC (with glyoxylate as cosubstrate) {ECO:0000269|PubMed:19264755};
CC Vmax=11.9 umol/min/mg enzyme toward pyruvate in the forward reaction
CC {ECO:0000269|PubMed:19264755};
CC Vmax=10.9 umol/min/mg enzyme toward glyoxylate in the forward
CC reaction {ECO:0000269|PubMed:19264755};
CC Vmax=17.4 umol/min/mg enzyme toward alanine in the reverse reaction
CC (with succinic semialdehyde as cosubstrate)
CC {ECO:0000269|PubMed:19264755};
CC Vmax=15.8 umol/min/mg enzyme toward alanine in the reverse reaction
CC (with glyoxylate as cosubstrate) {ECO:0000269|PubMed:19264755};
CC Vmax=12.1 umol/min/mg enzyme toward succinic semialdehyde in the
CC reverse reaction {ECO:0000269|PubMed:19264755};
CC Vmax=13.6 umol/min/mg enzyme toward glyoxylate in the reverse
CC reaction {ECO:0000269|PubMed:19264755};
CC pH dependence:
CC Optimum pH is 9.0 in the forward reaction.
CC {ECO:0000269|PubMed:19264755};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12859897,
CC ECO:0000269|PubMed:19264755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94CE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94CE5-2; Sequence=VSP_042907;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems, leaves,
CC shoots and roots. Detected in reproductive tissues, in the stigma,
CC style, abscission zone of siliques, stamens and pollen. Not found in
CC pollen tubes or the transmitting tract. In vegetative tissues, found in
CC dark-grown hypocotyls, leaves, guard cells and primary roots, including
CC the root tips and the elongation zones. Not found in the division zone
CC of the root. Expressed in the outermost layer of the shoot apical
CC meristem (SAM) (PubMed:21690177). {ECO:0000269|PubMed:18077464,
CC ECO:0000269|PubMed:21471118, ECO:0000269|PubMed:21690177}.
CC -!- INDUCTION: Not induced by hypoxia. Up-regulated by salt stress.
CC {ECO:0000269|PubMed:20122158}.
CC -!- DISRUPTION PHENOTYPE: No vegetative phenotype. Oversensitivity to ionic
CC stress but not to osmotic stress. Sustained roots growth upon treatment
CC with E-2-hexenal. Increased gamma-amino butyric acid (GABA) in leaves
CC and flowers and defects in pollen tube growth, guidance and fertility.
CC Cell elongation defects. Suppresses partially the ENF1 disruption
CC pleiotropic developmental phenotypes (including abaxialized and
CC adaxialized leaves). Enlarged expressing region of FIL, thus leading to
CC an increase in the size of leaf abaxial region associated with altered
CC GABA and SucA levels in shoots; however, the enf1 gabat1 double mutant
CC has a restored almost normal FIL expression pattern (PubMed:21690177).
CC {ECO:0000269|PubMed:12859897, ECO:0000269|PubMed:18077464,
CC ECO:0000269|PubMed:18846220, ECO:0000269|PubMed:20122158,
CC ECO:0000269|PubMed:21471118, ECO:0000269|PubMed:21690177}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF351125; AAK52899.1; -; mRNA.
DR EMBL; AP001306; BAB03068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76602.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76603.1; -; Genomic_DNA.
DR EMBL; AY034923; AAK59430.1; -; mRNA.
DR EMBL; AY142571; AAN13140.1; -; mRNA.
DR EMBL; AK317625; BAH20287.1; -; mRNA.
DR RefSeq; NP_001189947.1; NM_001203018.1. [Q94CE5-2]
DR RefSeq; NP_566700.1; NM_113117.4. [Q94CE5-1]
DR AlphaFoldDB; Q94CE5; -.
DR SMR; Q94CE5; -.
DR BioGRID; 7116; 3.
DR STRING; 3702.AT3G22200.2; -.
DR PaxDb; Q94CE5; -.
DR PRIDE; Q94CE5; -.
DR ProteomicsDB; 248481; -. [Q94CE5-1]
DR EnsemblPlants; AT3G22200.1; AT3G22200.1; AT3G22200. [Q94CE5-1]
DR EnsemblPlants; AT3G22200.2; AT3G22200.2; AT3G22200. [Q94CE5-2]
DR GeneID; 821784; -.
DR Gramene; AT3G22200.1; AT3G22200.1; AT3G22200. [Q94CE5-1]
DR Gramene; AT3G22200.2; AT3G22200.2; AT3G22200. [Q94CE5-2]
DR KEGG; ath:AT3G22200; -.
DR Araport; AT3G22200; -.
DR TAIR; locus:2090414; AT3G22200.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_4_1_1; -.
DR OMA; REGLNQH; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q94CE5; -.
DR BioCyc; MetaCyc:AT3G22200-LER-MON; -.
DR BRENDA; 2.6.1.19; 399.
DR BRENDA; 2.6.1.96; 399.
DR PRO; PR:Q94CE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94CE5; baseline and differential.
DR Genevisible; Q94CE5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IMP:CACAO.
DR GO; GO:0034387; F:4-aminobutyrate:pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0102351; F:gamma-aminobutyrate transaminase (glyoxylate dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0009943; P:adaxial/abaxial axis specification; IMP:UniProtKB.
DR GO; GO:0019484; P:beta-alanine catabolic process; IMP:TAIR.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:TAIR.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:TAIR.
DR GO; GO:0006540; P:glutamate decarboxylation to succinate; IMP:TAIR.
DR GO; GO:0006536; P:glutamate metabolic process; IMP:TAIR.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:TAIR.
DR GO; GO:0006020; P:inositol metabolic process; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:UniProtKB.
DR GO; GO:0009865; P:pollen tube adhesion; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0010033; P:response to organic substance; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0006105; P:succinate metabolic process; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IMP:TAIR.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..504
FT /note="Gamma-aminobutyrate transaminase POP2,
FT mitochondrial"
FT /id="PRO_0000416847"
FT BINDING 158..159
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 298
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 363..364
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT MOD_RES 327
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT VAR_SEQ 1..15
FT /note="MVVINSLRRLARTTQ -> MPTIVNKNLIFFQNAKLTWIRMKK (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042907"
FT MUTAGEN 98
FT /note="C->Y: In her1-1; loss of E2-hexenal responses."
FT /evidence="ECO:0000269|PubMed:17971036"
FT MUTAGEN 103
FT /note="G->N: In her1-2; loss of E2-hexenal responses."
FT /evidence="ECO:0000269|PubMed:17971036"
FT MUTAGEN 271
FT /note="G->E: In pop2-6; Loss of activity and complete
FT sterility."
FT /evidence="ECO:0000269|PubMed:18846220"
FT MUTAGEN 312
FT /note="G->D: In pop2-7; loss of activity."
FT /evidence="ECO:0000269|PubMed:18846220"
FT CONFLICT 21
FT /note="K -> R (in Ref. 1; AAK52899)"
FT /evidence="ECO:0000305"
SQ 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
