ID A0A1F5C8Z7_9BACT Unreviewed; 314 AA.
AC A0A1F5C8Z7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OGD39342.1};
DE Flags: Fragment;
GN ORFNames=A2V45_15490 {ECO:0000313|EMBL:OGD39342.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_58_17.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797275 {ECO:0000313|EMBL:OGD39342.1, ECO:0000313|Proteomes:UP000178644};
RN [1] {ECO:0000313|EMBL:OGD39342.1, ECO:0000313|Proteomes:UP000178644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGD39342.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MEYD01000036; OGD39342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5C8Z7; -.
DR STRING; 1797275.A2V45_15490; -.
DR Proteomes; UP000178644; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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;
FT DOMAIN 6..287
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
FT NON_TER 314
FT /evidence="ECO:0000313|EMBL:OGD39342.1"
SQ SEQUENCE 314 AA; 33515 MW; ECE09DC31A6891BA CRC64;
MSEISDFRSD TVTRPTPGMR RAMAEAAVGD DVLGDDPTVQ ELETLAAGIV GKEAALFVPS
GTMGNSVAVK AWTRELEEVI VEARSHIFNM ESTHLTFISR VTPRPLGSRR GAMDPDEVEA
NIRKPSVHTP ETSLVCVENT HNNWSGAVLP LANLKALRSV ADKHQIRIHM DGARIFNAST
ASGIPVKDYA ALSDSVMFCL SKGLSAPVGS MLAGPRDFID YARRIRKALG GGMRQAGVLA
APGLIALTEM VGRLGQDHAR AKKLASAIAG LPGVKLDPAD VETNIIIFGL SHPRVSIAEF
IAGLRKKRIL ALAL
//
