AGT_DROME
ID AGT_DROME Reviewed; 394 AA.
AC Q9W3Z3; C6TP18; Q8T0J1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000255|PIRNR:PIRNR000524};
DE Short=AGT {ECO:0000305};
DE EC=2.6.1.44 {ECO:0000255|PIRNR:PIRNR000524, ECO:0000269|PubMed:12220660};
GN Name=Agxt {ECO:0000303|PubMed:29980178, ECO:0000312|FlyBase:FBgn0014031};
GN Synonyms=Spat {ECO:0000312|FlyBase:FBgn0014031};
GN ORFNames=CG3926 {ECO:0000312|FlyBase:FBgn0014031};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL39372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head {ECO:0000312|EMBL:AAL39372.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ACU24744.1, ECO:0000312|EMBL:AFC38910.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACU24744.1, ECO:0000312|EMBL:AFC38910.1};
RC TISSUE=Head {ECO:0000312|EMBL:ACU24744.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=12220660; DOI=10.1016/s0014-5793(02)03229-5;
RA Han Q., Li J.;
RT "Comparative characterization of Aedes 3-hydroxykynurenine
RT transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate
RT aminotransferase.";
RL FEBS Lett. 527:199-204(2002).
RN [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=29980178; DOI=10.1186/s12882-018-0980-8;
RA Yang H., Male M., Li Y., Wang N., Zhao C., Jin S., Hu J., Chen Z., Ye Z.,
RA Xu H.;
RT "Efficacy of Hydroxy-L-proline (HYP) analogs in the treatment of primary
RT hyperoxaluria in Drosophila Melanogaster.";
RL BMC Nephrol. 19:167-167(2018).
CC -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate-dependent transamination
CC of alanine with glyoxylate as an amino group acceptor
CC (PubMed:12220660). Can also catalyze, although with much less
CC efficiency, the transamination of amino-butyrate, phenylalanine and
CC serine with glyoxylate or pyruvate as an amino group acceptor
CC (PubMed:12220660). Does not catalyze the transamination of both 3-
CC hydroxykynurenine and L-kynurenine (PubMed:12220660). May play a role
CC in the detoxification of glyoxylate, a toxic plant metabolite from the
CC fly diet (Probable). {ECO:0000269|PubMed:12220660,
CC ECO:0000305|PubMed:12220660}.
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 Evidence={ECO:0000255|PIRNR:PIRNR000524,
CC ECO:0000269|PubMed:12220660};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|PIRNR:PIRNR000524,
CC ECO:0000255|RuleBase:RU004504};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64 mM for glyoxylate (at 50 degrees Celsius, pH 7 and with alanine
CC as cosubstrate) {ECO:0000269|PubMed:12220660};
CC KM=149 mM for alanine (at 50 degrees Celsius, pH 7 and with
CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:12220660};
CC Vmax=170 umol/min/mg enzyme toward glyoxylate (at 50 degrees Celsius,
CC pH 7 and with alanine as cosubstrate) {ECO:0000269|PubMed:12220660};
CC Vmax=197 umol/min/mg enzyme toward alanine (at 50 degrees Celsius, pH
CC 7 and with glyoxylate as cosubstrate) {ECO:0000269|PubMed:12220660};
CC Note=kcat is 6800 min(-1) for glyoxylate (at 50 degrees Celsius, pH 7
CC and with alanine as cosubstrate) (PubMed:12220660). kcat is 7880
CC min(-1) for alanine (at 50 degrees Celsius, pH 7 and with glyoxylate
CC as cosubstrate) (PubMed:12220660). {ECO:0000269|PubMed:12220660};
CC pH dependence:
CC Optimum pH is 9 with alanine and glyoxylate as substrates.
CC {ECO:0000269|PubMed:12220660};
CC Temperature dependence:
CC Optimum temperature is between 30 and 80 degrees Celsius with alanine
CC and glyoxylate as substrates. {ECO:0000269|PubMed:12220660};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12220660}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P21549}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes accumulation of
CC calcium oxalate crystals in Malpighian tubules.
CC {ECO:0000269|PubMed:29980178}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|PIRNR:PIRNR000524,
CC ECO:0000255|RuleBase:RU004075}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39372.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL39372.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF46168.1; -; Genomic_DNA.
DR EMBL; AY069227; AAL39372.1; ALT_SEQ; mRNA.
DR EMBL; BT099504; ACU24744.1; -; mRNA.
DR EMBL; BT133279; AFC38910.1; -; mRNA.
DR RefSeq; NP_511062.1; NM_078507.2.
DR AlphaFoldDB; Q9W3Z3; -.
DR SMR; Q9W3Z3; -.
DR STRING; 7227.FBpp0070875; -.
DR PaxDb; Q9W3Z3; -.
DR EnsemblMetazoa; FBtr0070913; FBpp0070875; FBgn0014031.
DR GeneID; 31587; -.
DR KEGG; dme:Dmel_CG3926; -.
DR UCSC; CG3926-RA; d. melanogaster.
DR CTD; 31587; -.
DR FlyBase; FBgn0014031; Agxt.
DR VEuPathDB; VectorBase:FBgn0014031; -.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; Q9W3Z3; -.
DR OMA; KNWLPIM; -.
DR OrthoDB; 984738at2759; -.
DR PhylomeDB; Q9W3Z3; -.
DR Reactome; R-DME-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DME-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 31587; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31587; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0014031; Expressed in mouthpart and 18 other tissues.
DR ExpressionAtlas; Q9W3Z3; baseline and differential.
DR GO; GO:0005777; C:peroxisome; ISS:FlyBase.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:FlyBase.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:FlyBase.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Peroxisome; Pyridoxal phosphate; Pyruvate;
KW Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000452187"
FT BINDING 76..78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 204
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 259
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3LSM4"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|PIRSR:PIRSR000524-50"
FT CONFLICT 184
FT /note="L -> P (in Ref. 4; ACU24744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 43800 MW; FB4695B4733C1B11 CRC64;
MEVPPPLVLK RPLYVPSKTL MGPGPSNCSH RVLEAMSNPV LGHMHPECLQ IMDEVKEGIK
YIFQTLNDAT MCISGAGHSG MEAALCNLIE DGDVVLMGIT GVWGHRAGDM ARRYGAEVHY
VEASFGRALS HEEITFAFEA HRPKVFFIAQ GDSSTGIIQQ NIRELGELCR KYDCFLIVDT
VASLGGTEFL MDEWKVDVAY TGSQKSLGGP AGLTPISFSK RALTRIRKRK TKPKVYYFDI
LLIGQYWGCY GTPRIYHHTI SSTLLYGLRE ALAHFCAVGL KAVVRRHQEC SKRLQLGIEE
LGLEMFVSRE EERLPTVNTI KVPFGVDWKK VAEYAMRKYS VEISGGLGPT VEHVFRIGLM
GENATVERVD MVLSILNEAI QSSKLGIKTD LSKI
