ID D8FZB8_9CYAN Unreviewed; 372 AA.
AC D8FZB8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase family {ECO:0000313|EMBL:CBN55708.1};
GN ORFNames=OSCI_2320013 {ECO:0000313|EMBL:CBN55708.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN55708.1, 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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CACA01000201; CBN55708.1; -; Genomic_DNA.
DR RefSeq; WP_007354926.1; NZ_CACA01000201.1.
DR AlphaFoldDB; D8FZB8; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBN55708.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000313|EMBL:CBN55708.1}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 372 AA; 41748 MW; 20DD51B411B1025F CRC64;
MSAPIPVNQP LLDGNERQYL NQCIDSGWIS SEGPFVKRFE EEFAVRVGRQ YGIAVCNGSA
ALDAAVAALK IGPGDEVIVP TFTIISCVAA IVRAGAKPVL VDCDRETWNM DIAQITTKIS
PQTKAIMAVH IYGLPVNITP LLDLAKRYNL QIIEDAAEMH GQTYKNQPCG SFGDISTFSF
YPNKHITTGE GGMIVTDDAK LAERCRSLRN LCFQPQQRFV HEELGWNLRM SNIQAALGIA
QLERLDEFVA RKRRMGYIYN QLLADISGLE LPLAFTTYAK NIYWVYGVVL KDELPFDAVE
AIRRLAEHQI GTRPFFWPMH EQPIFKKMGL FQGESYPVAE RLARRGFYIP SGIALTDTQM
ERVAQVIKEV IR
//
