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Database: UniProt
Entry: A0A2T1D326_9CYAN
LinkDB: A0A2T1D326_9CYAN
Original site: A0A2T1D326_9CYAN 
ID   A0A2T1D326_9CYAN        Unreviewed;       370 AA.
AC   A0A2T1D326;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:PSB14898.1};
GN   ORFNames=C7B65_25650 {ECO:0000313|EMBL:PSB14898.1};
OS   Phormidesmis priestleyi ULC007.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1920490 {ECO:0000313|EMBL:PSB14898.1, ECO:0000313|Proteomes:UP000238634};
RN   [1] {ECO:0000313|EMBL:PSB14898.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB14898.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB14898.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB14898.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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:PSB14898.1}.
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DR   EMBL; PVWG01000074; PSB14898.1; -; Genomic_DNA.
DR   RefSeq; WP_073075228.1; NZ_PVWG01000074.1.
DR   AlphaFoldDB; A0A2T1D326; -.
DR   STRING; 1920490.GCA_001895925_03335; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000238634; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:PSB14898.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238634};
KW   Transferase {ECO:0000313|EMBL:PSB14898.1}.
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         185
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   370 AA;  40787 MW;  7B2AD8E56380166B CRC64;
     MIPFIDLKAQ YLSIKDEIDT AVIKVLESTQ FILGSEVAAL EEEFAEYCSA EHGIAVNTGT
     SALHLALVAA GIGPGDEVIT VPFTFIATVA AIVYTGAKPV FVDIDPASYT IDVTQIEAAV
     TERTKAILPV HLYGQAADMD PILEIAQRHN LIVIEDAAQA HRAEYKGRRV GSIGDIGCFS
     FYPGKNLGAY GEGGMVTTNN AEFDSTIRML RDWGQERRYN HVLKGYNYRM DGIQGAILRI
     KLRYLDQWTE ARRAHATQYD QLLKDSTVKT PVVMPYSHHV YHIYAVRVGD RTALQQKLSE
     QGIQTGIHYP IPVHLQPAYS DLGYQPGAFP YSESTAREVL SLPMYPELTP EQVDAVAQSL
     HSLSQGAQVS
//
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