AGT21_ARATH
ID AGT21_ARATH Reviewed; 476 AA.
AC Q940M2; Q9SU41; Q9SWE2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial;
DE EC=2.6.1.44;
DE AltName: Full=Beta-alanine-pyruvate aminotransferase 1;
DE Flags: Precursor;
GN Name=AGT2; OrderedLocusNames=At4g39660; ORFNames=T19P19.50;
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].
RC STRAIN=cv. Columbia;
RX PubMed=12529529; DOI=10.1104/pp.011460;
RA Liepman A.H., Olsen L.J.;
RT "Alanine aminotransferase homologs catalyze the glutamate:glyoxylate
RT aminotransferase reaction in peroxisomes of Arabidopsis.";
RL Plant Physiol. 131:215-227(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80629.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF166351; AAD48837.1; -; mRNA.
DR EMBL; AL022605; CAA18752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80629.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87100.1; -; Genomic_DNA.
DR EMBL; AY054264; AAL06923.1; -; mRNA.
DR EMBL; BT002306; AAN73303.1; -; mRNA.
DR PIR; T05003; T05003.
DR RefSeq; NP_568064.1; NM_120126.5.
DR AlphaFoldDB; Q940M2; -.
DR SMR; Q940M2; -.
DR BioGRID; 15400; 1.
DR STRING; 3702.AT4G39660.1; -.
DR PaxDb; Q940M2; -.
DR PRIDE; Q940M2; -.
DR ProteomicsDB; 244783; -.
DR EnsemblPlants; AT4G39660.1; AT4G39660.1; AT4G39660.
DR GeneID; 830120; -.
DR Gramene; AT4G39660.1; AT4G39660.1; AT4G39660.
DR KEGG; ath:AT4G39660; -.
DR Araport; AT4G39660; -.
DR TAIR; locus:2135237; AT4G39660.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_10_0_1; -.
DR InParanoid; Q940M2; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q940M2; -.
DR BioCyc; ARA:AT4G39660-MON; -.
DR PRO; PR:Q940M2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q940M2; baseline and differential.
DR Genevisible; Q940M2; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IBA:GO_Central.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 Aminotransferase; Mitochondrion; Photorespiration; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..476
FT /note="Alanine--glyoxylate aminotransferase 2 homolog 1,
FT mitochondrial"
FT /id="PRO_0000041945"
FT MOD_RES 320
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 240
FT /note="H -> Q (in Ref. 1; AAD48837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 51953 MW; 9E5ABC10C3C2EC83 CRC64;
MALQRQLLKR ATSDIYHRRA ISLLRTDFST SPSIADAPPH IPPFVHQPRP YKGPSADEVL
QKRKKFLGPS LFHYYQKPLN IVEGKMQYLY DESGRRYLDA FAGIVTVSCG HCHPDILNAI
TEQSKLLQHA TTIYLHHAIG DFAEALAAKM PGNLKVVYFV NSGSEANELA MMMARLYTGS
LEMISLRNAY HGGSSNTIGL TALNTWKYPL PQGEIHHVVN PDPYRGVFGS DGSLYAKDVH
DHIEYGTSGK VAGFIAETIQ GVGGAVELAP GYLKSVYEIV RNAGGVCIAD EVQTGFGRTG
SHYWGFQTQD VVPDIVTMAK GIGNGLPLGA VVTTPEIASV LASKILFNTF GGNPVCSAGG
LAVLNVIDKE KRQEHCAEVG SHLIQRLKDV QKRHDIIGDV RGRGLMVGIE LVSDRKDKTP
AKAETSVLFE QLRELGILVG KGGLHGNVFR IKPPMCFTKD DADFLVDALD YSISRL
