ID A2CA79_PROM3 Unreviewed; 394 AA.
AC A2CA79;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Serine:pyruvate/alanine:glyoxylate aminotransferase {ECO:0000313|EMBL:ABM78389.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:ABM78389.1};
GN Name=spt {ECO:0000313|EMBL:ABM78389.1};
GN OrderedLocusNames=P9303_16451 {ECO:0000313|EMBL:ABM78389.1};
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78389.1, ECO:0000313|Proteomes:UP000002274};
RN [1] {ECO:0000313|EMBL:ABM78389.1, ECO:0000313|Proteomes:UP000002274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78389.1,
RC ECO:0000313|Proteomes:UP000002274};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP000554; ABM78389.1; -; Genomic_DNA.
DR AlphaFoldDB; A2CA79; -.
DR STRING; 59922.P9303_16451; -.
DR KEGG; pmf:P9303_16451; -.
DR HOGENOM; CLU_027686_0_0_3; -.
DR BioCyc; PMAR59922:G1G80-1431-MONOMER; -.
DR Proteomes; UP000002274; Chromosome.
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:ABM78389.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:ABM78389.1};
KW Transferase {ECO:0000313|EMBL:ABM78389.1}.
FT DOMAIN 56..366
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 394 AA; 43019 MW; 611C5633C308E7D9 CRC64;
MATTQTLPQV DQSHKTVLEP IATPTRLLFG PGPSNADPKV LQALARSPIG HLDPLYLELM
GEVQELLRYT WQTDNRFTLP MSGTGSAAME ATLTNTVEPG DTVLVAVNGY FGNRLADMAG
RYRANVQLIE KPWGEAFSLA ELEAALIEHR PAILALVHAE TSTGVCQPMD GVGDLCHKHD
CLLLLDTVTS LGAVPVFLDQ WKVDLSYSCS QKGLSCPPGL GPFTMGPRAE EKLSARSGKV
PNWYLDVSLL NQYWGSDRVY HHTAPVNMNF GMREALRLLA DEGLENAWDR HRCNAEALWA
GLESLGLELH VPEALRLPTL TTVCIPNGVD GNAFRLHLLN EHGIEIGGGL GSLAGKIWRI
GLMGYNSTPK NVELLLNLFE SELPRFRENV AVAA
//
