ID Q7V1F4_PROMP Unreviewed; 394 AA.
AC Q7V1F4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE SubName: Full=Serine:pyruvate/alanine:glyoxylate aminotransferase {ECO:0000313|EMBL:CAE19378.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:CAE19378.1};
GN Name=agt {ECO:0000313|EMBL:CAE19378.1};
GN Synonyms=spt {ECO:0000313|EMBL:CAE19378.1};
GN OrderedLocusNames=PMM0919 {ECO:0000313|EMBL:CAE19378.1};
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE19378.1, ECO:0000313|Proteomes:UP000001026};
RN [1] {ECO:0000313|EMBL:CAE19378.1, ECO:0000313|Proteomes:UP000001026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4
RC {ECO:0000313|Proteomes:UP000001026};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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}.
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DR EMBL; BX548174; CAE19378.1; -; Genomic_DNA.
DR RefSeq; WP_011132552.1; NC_005072.1.
DR AlphaFoldDB; Q7V1F4; -.
DR STRING; 59919.PMM0919; -.
DR KEGG; pmm:PMM0919; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_3; -.
DR OMA; IRINHMG; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000001026; 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; 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 Aminotransferase {ECO:0000313|EMBL:CAE19378.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:CAE19378.1};
KW Transferase {ECO:0000313|EMBL:CAE19378.1}.
FT DOMAIN 48..375
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; 44115 MW; 9769C5F67631D7A3 CRC64;
MTETKLISTL NKENLPHLDK TYVPSRLLLG PGPSNANPEV LKALALNPIG HLDEAYIELM
SEVQKLLRYT WQCNNRITLP MSGTGSAAME ASIANFIEPG EKILIAKKGY FGDRLVDMAS
RYNADVSVIE KEWGEAFTFE EIKYEIETKK PVIFAIVHAE TSTGVLQPLE GIGDLCRKNN
CLFLVDAVTS LGALELFIDD WKIDLAYSCS QKGLSCPPGL SPFTMNKRAE DKLSARTSKV
PNWYLDLSLL NRYWGSDRVY HHTAPVNMNF AIREGLRLIA NEGLENIWRR HNSNAIKLWK
GLESLGMDLH VSSEFRLPTL TTVKIPPAVD GDAYRNHLLK NFGIEIGNGL GALSGKVWRI
GLMGFNSNEE NVDRLLNLFD TELKKFSIFD SSSF
//