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AGT2L_DROME
ID   AGT2L_DROME             Reviewed;         494 AA.
AC   Q9VU95; Q95RV4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Alanine--glyoxylate aminotransferase 2-like {ECO:0000250|UniProtKB:Q8TBG4};
DE            EC=4.2.3.- {ECO:0000305};
GN   ORFNames=CG8745;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
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]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q8TBG4};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to possess aminotransferase activity.
CC       {ECO:0000250|UniProtKB:Q8TBG4}.
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DR   EMBL; AE014296; AAF49794.2; -; Genomic_DNA.
DR   EMBL; AY061111; AAL28659.1; -; mRNA.
DR   RefSeq; NP_648665.1; NM_140408.3.
DR   AlphaFoldDB; Q9VU95; -.
DR   SMR; Q9VU95; -.
DR   BioGRID; 64872; 15.
DR   IntAct; Q9VU95; 2.
DR   STRING; 7227.FBpp0075543; -.
DR   PaxDb; Q9VU95; -.
DR   PRIDE; Q9VU95; -.
DR   DNASU; 39530; -.
DR   EnsemblMetazoa; FBtr0075801; FBpp0075543; FBgn0036381.
DR   GeneID; 39530; -.
DR   KEGG; dme:Dmel_CG8745; -.
DR   UCSC; CG8745-RA; d. melanogaster.
DR   FlyBase; FBgn0036381; CG8745.
DR   VEuPathDB; VectorBase:FBgn0036381; -.
DR   eggNOG; KOG1403; Eukaryota.
DR   GeneTree; ENSGT00940000171040; -.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   InParanoid; Q9VU95; -.
DR   OMA; MVPNYNP; -.
DR   OrthoDB; 145181at2759; -.
DR   PhylomeDB; Q9VU95; -.
DR   Reactome; R-DME-1442490; Collagen degradation.
DR   Reactome; R-DME-1483213; Synthesis of PE.
DR   Reactome; R-DME-71064; Lysine catabolism.
DR   BioGRID-ORCS; 39530; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39530; -.
DR   PRO; PR:Q9VU95; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036381; Expressed in spermathecum and 37 other tissues.
DR   Genevisible; Q9VU95; DM.
DR   GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; ISS:FlyBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0035094; P:response to nicotine; IEP:FlyBase.
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   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..494
FT                   /note="Alanine--glyoxylate aminotransferase 2-like"
FT                   /id="PRO_0000287669"
FT   MOD_RES         291
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54284 MW;  152844D2C5C168B5 CRC64;
     MPFAHEQLNL VASEQLSKTE TIKLRNQHIG QACQLFYRSD PLKIVRGQGQ YMFDEEGTRY
     LDCINNVAHV GHCHPEVVRA GALQMATIST NNRFLHDELV QCARTLTSKM PEPLSVCFFV
     NSGSEANDLA LRLARNFTKR QDVITLDHAY HGHLQSVMEV SPYKFNQPGG EAKPDYVHVA
     PCPDVYGGKF TDKMYPDADM GALYAQPIEE ICQKQLAKGQ GVAAFIAESL QSCGGQILPP
     AGYFQAVYDA VRSAGGVCIA DEVQVGFGRV GSHYWAFETQ NVIPDIVCVA KPMGNGHPVG
     AVVTTPEIAQ AFHATGVAYF NTYGGNPVSC AIANAVMRVI EEEGLQQKAL VLGDYLLEEC
     NRLKQEFECI GDVRGAGLFV GIELVQDRKE RIPDKKAAHW VVNRMKQLHR VLVSSDGPND
     NVIKLKPPMC FNRENADEFL LGFRECLTAV MQERLASATS AAMAATSGVI ATATETLANK
     TKLFERQDRL IKSV
 
 
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