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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//