AGT_AEDAE
ID AGT_AEDAE Reviewed; 393 AA.
AC Q3LSM4; Q16FD8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000255|PIRNR:PIRNR000524, ECO:0000303|PubMed:16681462};
DE EC=2.6.1.44 {ECO:0000255|PIRNR:PIRNR000524, ECO:0000269|PubMed:16681462};
GN Name=AGT {ECO:0000303|PubMed:16681462};
GN ORFNames=AAEL010480 {ECO:0000312|EMBL:EAT37540.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000312|Proteomes:UP000008820};
RN [1] {ECO:0000312|EMBL:ABA26661.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16681462; DOI=10.1042/bj20060469;
RA Han Q., Kim S.R., Ding H., Li J.;
RT "Evolution of two alanine glyoxylate aminotransferases in mosquito.";
RL Biochem. J. 397:473-481(2006).
RN [2] {ECO:0000312|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000312|Proteomes:UP000008820}, and LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0007744|PDB:2HUF, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH L-ALANINE; PYRIDOXAL
RP PHOSPHATE AND GLYOXYLIC ACID, AND SUBUNIT.
RX PubMed=16990263; DOI=10.1074/jbc.m607032200;
RA Han Q., Robinson H., Gao Y.G., Vogelaar N., Wilson S.R., Rizzi M., Li J.;
RT "Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase.";
RL J. Biol. Chem. 281:37175-37182(2006).
CC -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate-dependent transamination
CC of alanine with glyoxylate as an amino group acceptor
CC (PubMed:16681462). Can also catalyze, although with much less
CC efficiency, the transamination of serine, and histidine with glyoxylate
CC and the and transamination of glycine with pyruvate as an amino group
CC acceptor (PubMed:16681462). Does not catalyze the transamination of
CC both 3-hydroxykynurenine and L-kynurenine (PubMed:16681462). May play a
CC role in the detoxification of glyoxylate, a toxic plant metabolite from
CC the pupae and adult diet (Probable). {ECO:0000269|PubMed:16681462,
CC ECO:0000305|PubMed:16681462}.
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:16681462};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|PIRNR:PIRNR000524,
CC ECO:0000255|RuleBase:RU004504, ECO:0000269|PubMed:16990263};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 mM for alanine (at 45 degrees Celsius, pH 7.5 and with
CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:16681462};
CC Note=kcat is 117 sec(-1) for alanine (at 45 degrees Celsius, pH 7.5
CC and with glyoxylate as cosubstrate). {ECO:0000269|PubMed:16681462};
CC pH dependence:
CC Optimum pH is 9 (PubMed:16681462). Active between pH 7-10 (for
CC alanine and glyoxylate as substrates) (PubMed:16681462).
CC {ECO:0000269|PubMed:16681462};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius (PubMed:16681462). Maximum
CC activity between 50 and 80 degrees Celsius (for alanine and
CC glyoxylate as substrates) (PubMed:16681462).
CC {ECO:0000269|PubMed:16681462};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16990263}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P21549}.
CC -!- TISSUE SPECIFICITY: Expressed in head and abdomen of adult females.
CC {ECO:0000269|PubMed:17510324}.
CC -!- DEVELOPMENTAL STAGE: Expressed at pupal and adult stages (at protein
CC level). {ECO:0000269|PubMed:16681462}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|PIRNR:PIRNR000524,
CC ECO:0000255|RuleBase:RU004075}.
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DR EMBL; DQ182329; ABA26661.1; -; mRNA.
DR EMBL; CH478461; EAT32945.1; -; Genomic_DNA.
DR EMBL; CH477665; EAT37540.1; -; Genomic_DNA.
DR RefSeq; XP_001649636.1; XM_001649586.1.
DR RefSeq; XP_001660875.1; XM_001660825.1.
DR PDB; 2HUF; X-ray; 1.75 A; A/B=1-393.
DR PDB; 2HUI; X-ray; 1.75 A; A/B=1-393.
DR PDB; 2HUU; X-ray; 2.10 A; A/B=1-393.
DR PDBsum; 2HUF; -.
DR PDBsum; 2HUI; -.
DR PDBsum; 2HUU; -.
DR AlphaFoldDB; Q3LSM4; -.
DR SMR; Q3LSM4; -.
DR STRING; 7159.AAEL014817-PA; -.
DR GeneID; 5573438; -.
DR KEGG; aag:5573438; -.
DR VEuPathDB; VectorBase:AAEL010480; -.
DR eggNOG; KOG2862; Eukaryota.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; Q3LSM4; -.
DR OMA; KNWLPIM; -.
DR OrthoDB; 984738at2759; -.
DR PhylomeDB; Q3LSM4; -.
DR EvolutionaryTrace; Q3LSM4; -.
DR Proteomes; UP000008820; Chromosome 1.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
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 3D-structure; Aminotransferase; Peroxisome; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Alanine--glyoxylate aminotransferase"
FT /id="PRO_0000452186"
FT BINDING 78..80
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:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUF, ECO:0007744|PDB:2HUI,
FT ECO:0007744|PDB:2HUU"
FT BINDING 155
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUI"
FT BINDING 155
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUU"
FT BINDING 205
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:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU"
FT BINDING 257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU"
FT BINDING 260
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU"
FT BINDING 356
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:16990263,
FT ECO:0007744|PDB:2HUI"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|PIRSR:PIRSR000524-50,
FT ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI,
FT ECO:0007744|PDB:2HUU"
FT CONFLICT 16
FT /note="V -> I (in Ref. 2; EAT32945)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:2HUF"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2HUF"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2HUF"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 281..301
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:2HUF"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:2HUF"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2HUF"
FT HELIX 366..383
FT /evidence="ECO:0007829|PDB:2HUF"
SQ SEQUENCE 393 AA; 43109 MW; C392C8742CFCA986 CRC64;
MEYKVTPPAV LREPLVTPNK LLMGPGPSNA PQRVLDAMSR PILGHLHPET LKIMDDIKEG
VRYLFQTNNI ATFCLSASGH GGMEATLCNL LEDGDVILIG HTGHWGDRSA DMATRYGADV
RVVKSKVGQS LSLDEIRDAL LIHKPSVLFL TQGDSSTGVL QGLEGVGALC HQHNCLLIVD
TVASLGGAPM FMDRWEIDAM YTGSQKVLGA PPGITPVSFS HRAVERYKRR NTKVKVYYWD
MSLVGDYWGC FGRPRIYHHT ISSTLLYGLR EAIAMACEEG LPALIARHED CAKRLYRGLQ
DAGFELYADP KDRLSTVTTI KVPQGVDWLK AAQYAMKTYL VEISGGLGPT AGQVFRIGLM
GQNATTERVD RVLQVFQEAV AAVKPDVQVK GKM
