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Database: UniProt
Entry: A0A2P6U326_CHLSO
LinkDB: A0A2P6U326_CHLSO
Original site: A0A2P6U326_CHLSO 
ID   A0A2P6U326_CHLSO        Unreviewed;       401 AA.
AC   A0A2P6U326;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=alanine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00013049};
DE            EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
GN   ORFNames=C2E21_1145 {ECO:0000313|EMBL:PRW60716.1};
OS   Chlorella sorokiniana (Freshwater green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW60716.1, ECO:0000313|Proteomes:UP000239899};
RN   [1] {ECO:0000313|EMBL:PRW60716.1, ECO:0000313|Proteomes:UP000239899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX   PubMed=29178410; DOI=10.1111/tpj.13789;
RA   Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA   Barney B.M.;
RT   "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT   conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL   Plant J. 93:566-586(2018).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRW60716.1}.
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DR   EMBL; LHPG02000002; PRW60716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6U326; -.
DR   STRING; 3076.A0A2P6U326; -.
DR   OrthoDB; 1010571at2759; -.
DR   Proteomes; UP000239899; 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; 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   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   PANTHER; PTHR21152:SF24; SERINE--PYRUVATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239899}.
FT   DOMAIN          56..358
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   401 AA;  43644 MW;  AEEB6CB0290EE841 CRC64;
     MAFTSQRPGE PTPPISDAHR GPTGVLEVPQ RFLMGPGPAN AEPRILNAQS LPLLGHMHPP
     FLKIMDEVQQ GLRYLFQTDS KYTLCASGTG HSGMEMAIAN LLEPGEKILV GNNGIWGTRV
     ADMAGRFGAE VVELKTEAGT SFSLDTLTAA VEKEKPAVLF LCQGESSTGV HQTLAGVGDL
     CRKHNVLLLV DTVCSLGGVP LYADAWKVDA IYSGSQKCLS APPGAAPLML NDRALEKVRA
     RKTKVRSYYF DLNLVGDYWG WFNSRSYHHT GMTSMWYAMR EALAIVAEQG LESMWERHEA
     AHKQLWEGLS ALGLQPFVEK PEDRLVTVNT IKVPEGIDWA AVSKNAMDKF NVEIAGGLGP
     TAGKIWRVGL MGYNAKPANV ELVLAAFKDG LRQQGWELAA N
//
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