ID K9TA81_9CYAN Unreviewed; 341 AA.
AC K9TA81;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AFY78919.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:AFY78919.1};
GN ORFNames=Ple7327_3743 {ECO:0000313|EMBL:AFY78919.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY78919.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY78919.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY78919.1,
RC ECO:0000313|Proteomes:UP000010382};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; CP003590; AFY78919.1; -; Genomic_DNA.
DR AlphaFoldDB; K9TA81; -.
DR STRING; 118163.Ple7327_3743; -.
DR KEGG; plp:Ple7327_3743; -.
DR PATRIC; fig|118163.3.peg.4180; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_3; -.
DR Proteomes; UP000010382; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AFY78919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010382}.
FT DOMAIN 4..287
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 341 AA; 37026 MW; B1A83D805E952FCB CRC64;
MIIDLRSDTI TKPTPAMREA MAKAEVGDDV FGDDPTVNAL EAYVAELLGK EEAVYMPSGT
MTNQVALRVH TEPGDEVILE SEAHIYYYEG GAPAALSGVM CRLIKGNKGI FSATDVERVL
RPDNYHFPKT KLVCLENTHN RGGGRIFPLS EIEAIAHICQ ERNLKLHLDG ARLWNACAAT
SISEADYAKP FDTVSVCFSK GLGAPVGSAL VGSKELIKRA RRFRKMFGGG MRQAGIIAAG
ALYGLKHHRE RLLEDHVNAK ILAKGLQQID GIAIDPEDVQ TNIVIFQTKA IPAETLAQNL
QEKGVALLAI GSHSLRAVTN LMVTQEQIQA VPELVEAAMR S
//
