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Database: UniProt
Entry: B0W8F7_CULQU
LinkDB: B0W8F7_CULQU
Original site: B0W8F7_CULQU 
ID   B0W8F7_CULQU            Unreviewed;       397 AA.
AC   B0W8F7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000256|PIRNR:PIRNR000524};
DE            EC=2.6.1.44 {ECO:0000256|PIRNR:PIRNR000524};
GN   Name=6034710 {ECO:0000313|EnsemblMetazoa:CPIJ002835-PA};
GN   ORFNames=CpipJ_CPIJ002835 {ECO:0000313|EMBL:EDS38886.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS38886.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS38886.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ002835-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ002835-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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:0000256|PIRNR:PIRNR000524};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRNR:PIRNR000524, ECO:0000256|PIRSR:PIRSR000524-50};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|PIRNR:PIRNR000524}.
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DR   EMBL; DS231858; EDS38886.1; -; Genomic_DNA.
DR   RefSeq; XP_001844991.1; XM_001844939.1.
DR   AlphaFoldDB; B0W8F7; -.
DR   STRING; 7176.B0W8F7; -.
DR   EnsemblMetazoa; CPIJ002835-RA; CPIJ002835-PA; CPIJ002835.
DR   KEGG; cqu:CpipJ_CPIJ002835; -.
DR   VEuPathDB; VectorBase:CPIJ002835; -.
DR   VEuPathDB; VectorBase:CQUJHB008569; -.
DR   eggNOG; KOG2862; Eukaryota.
DR   HOGENOM; CLU_027686_0_0_1; -.
DR   InParanoid; B0W8F7; -.
DR   OMA; NHTGPRA; -.
DR   OrthoDB; 1010571at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   CDD; cd06451; AGAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EDS38886.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR000524}; Pyruvate {ECO:0000313|EMBL:EDS38886.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Transferase {ECO:0000313|EMBL:EDS38886.1}.
FT   DOMAIN          37..334
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   397 AA;  44584 MW;  AA244C682D49630C CRC64;
     MDTITPPVSL LKPMNIPEKI MMGPGPSNCS KRVLTALTNT SLSNFHAELF QVIDEVKDGI
     RYVFQTRNRT TMCISGSAHA AMEALLCNLL EEGERVLIAV NGIWAERAVE MATRYGADVR
     ILEGPDDKPF PLADLKKAIE QHKPKCLFVT HGDSSSGLLQ PLEELGRVCH ENDCLLLVDA
     VASLCGVPFY MDKWEIDGVY TGSQKVLGAP PGITPISISD KALAAIRARK TKSKVFYWDL
     LLLGNYWGCY DEQKMYHHTV SSNLIFALRE ALAQIVEEGL DAQIQRRQEC ARALYRGLSE
     MGLEIFIKNP KHRLSTVTGI MIPEGVTWWK VSQYAMKNLE IQGGLGPTWE KAWRVGIMGE
     CSTLQKVNYY LFAFRESLKA THPEYEFVEL KHQNGYH
//
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