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Database: UniProt
Entry: A0A0B4ECZ2_9RHOB
LinkDB: A0A0B4ECZ2_9RHOB
Original site: A0A0B4ECZ2_9RHOB 
ID   A0A0B4ECZ2_9RHOB        Unreviewed;       334 AA.
AC   A0A0B4ECZ2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=GC1_15850 {ECO:0000313|EMBL:KID08738.1};
OS   Leisingera sp. ANG1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID08738.1, ECO:0000313|Proteomes:UP000031201};
RN   [1] {ECO:0000313|EMBL:KID08738.1, ECO:0000313|Proteomes:UP000031201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG1 {ECO:0000313|EMBL:KID08738.1,
RC   ECO:0000313|Proteomes:UP000031201};
RX   PubMed=21551313; DOI=10.1128/JB.05139-11;
RA   Collins A.J., Nyholm S.V.;
RT   "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   J. Bacteriol. 193:3397-3398(2011).
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:KID08738.1}.
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DR   EMBL; AFCF02000008; KID08738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4ECZ2; -.
DR   STRING; 1002340.GC1_15850; -.
DR   eggNOG; COG2008; Bacteria.
DR   Proteomes; UP000031201; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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          3..279
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   334 AA;  34398 MW;  BB953C9CF9BD7C1F CRC64;
     MCDLRSDTVT RPDAGMLRAM AAAELGDDVF GEDPSVNRLE AALAERLGKA AGLFLPTGTM
     SNFTAMLAHC QRGEEVICGR GYHVNAYEAA GASVLGGIAL CPLPVRADGA LDPAEIRAAV
     KEDDPHLPIS RLLSLENTHN GLAVPLADMA AAAEAGRAAG LSVHLDGARF FNAVTALGCS
     ETDLAGLADT VSVCLSKGLG TPAGSVLVGP ADLIAKARRW RKMLGGGMRQ AGVLAAAGLY
     ALEHNAGRLA EDHARAAELA GVLRGLGAGD VSQATNMVFF TPGDGRNDDL RMHLAAEGLV
     IGGGNSGAIR MVLHKNVDDA ALAQMVQGLR RFYG
//
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