ID D8G1J5_9CYAN Unreviewed; 385 AA.
AC D8G1J5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Serine--glyoxylate transaminase {ECO:0000313|EMBL:CBN56485.1};
DE EC=2.6.1.45 {ECO:0000313|EMBL:CBN56485.1};
GN ORFNames=OSCI_3020048 {ECO:0000313|EMBL:CBN56485.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56485.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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; CACA01000267; CBN56485.1; -; Genomic_DNA.
DR RefSeq; WP_007355696.1; NZ_CACA01000267.1.
DR AlphaFoldDB; D8G1J5; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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: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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBN56485.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000313|EMBL:CBN56485.1}.
FT DOMAIN 27..329
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 385 AA; 41450 MW; B9968F5E9A7E8AEC CRC64;
MDNKLMLMIP GPTPVPEAAL LAMAKHPMGH RSSEFDAIFA ECTENLKWLH QTKSDVLSLT
VSGTGAMEAG IINFLSAGDR VLVGNNGKFG ERWGEVAQAY GLNAEIITAE WGQPLDPEKF
REKLEADTNK EIKAVIITHS ETSTGVLNDL ETINRHVKAH GEALIMVDAV TSLGAANVPM
DEWGIDVIAS GSQKAYMIPP GLGFVAVSPK AWEAYKTAKL PRFYLDLGKY RKDAAKNTTP
FTPPVNMFFG LQVTLRMMKA EGLENVFARH QRLMKTTHAA VKALGLGLLA ADGAASPAIT
AVAPPAEVDA QKVRSLMKKR FDILLADGQD HLKGKIFRIG HLGFVCDRDI LAAISALETV
LRELGYEGFS SGAGIAAAAK VLSES
//
