ID I3Z5C1_BELBD Unreviewed; 338 AA.
AC I3Z5C1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AFL84439.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:AFL84439.1};
GN OrderedLocusNames=Belba_1850 {ECO:0000313|EMBL:AFL84439.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL84439.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-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; CP003281; AFL84439.1; -; Genomic_DNA.
DR RefSeq; WP_014772419.1; NC_018010.1.
DR AlphaFoldDB; I3Z5C1; -.
DR STRING; 866536.Belba_1850; -.
DR KEGG; bbd:Belba_1850; -.
DR PATRIC; fig|866536.3.peg.1906; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_10; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000006050; 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:AFL84439.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006050}.
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 338 AA; 37093 MW; 1B6FD6CBA6ED37AB CRC64;
MIIDLRSDTL TKPTQGMLEA MWSAPVGDDV FGEDPTVNAL EQKLADMFGM ESGLFCPSGT
MTNQIAIRLH TGLQTEVICH KYSHIYLYEG GGIMSNSHAS VKLLDGAYGK ISPQDILDSV
NPDDVHAPET TLVSLENTMN KGGGSIYTLD EIKPIKAICE QYGLKLHLDG ARLFNALVES
GESPKDWGTM FDTISICLSK GLGCPVGSVL LGNKADIKRA RKVRKAFGGG MRQAGFLAAA
AIYALDHHID RLKEDHARAR KLGEMLEQHS LVSEVFPVMT NIVIAKLAGI TPAEMLLKLE
SEGIKAVKFG KDQVRFVTHL DFDDEMLERF EEKIIEIR
//
