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Database: UniProt
Entry: A0A1E7JV97_9ACTN
LinkDB: A0A1E7JV97_9ACTN
Original site: A0A1E7JV97_9ACTN 
ID   A0A1E7JV97_9ACTN        Unreviewed;       378 AA.
AC   A0A1E7JV97;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OEU94406.1};
GN   ORFNames=AN216_24500 {ECO:0000313|EMBL:OEU94406.1};
OS   Streptomyces oceani.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU94406.1, ECO:0000313|Proteomes:UP000176101};
RN   [1] {ECO:0000313|EMBL:OEU94406.1, ECO:0000313|Proteomes:UP000176101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU94406.1,
RC   ECO:0000313|Proteomes:UP000176101};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(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:OEU94406.1}.
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DR   EMBL; LJGU01000155; OEU94406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7JV97; -.
DR   STRING; 1075402.AN216_24500; -.
DR   PATRIC; fig|1075402.3.peg.1155; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000176101; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000176101}.
FT   DOMAIN          57..286
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   378 AA;  41591 MW;  D53054606497B865 CRC64;
     MAEEHEAVVR RRLAAWTGAT RKLSRGPVAG TLAERLDQLA REGAEAYDLS DWTDTYGNRV
     VAELERRTAE TLGTEAAAFF PTGTMAQQVA LRCWAGRTAN RTVAMHPLAH PEQWERDALS
     QLTGLRVVHP TQAPRMPYDS EVRALREPFG TLALELPLRE AGFLLPDWDE LTATVAVARE
     RDAVVHFDGA RLWECAPHFG RGLPEIAELA DSVYVSFYKS LGGLSGAALA GSAEFIEETT
     TWRHRYGGQL FQQWPAALSA LAGLDRELPR LPEYVARAKE VAEALRAGCT AAGVSWVRIQ
     PEVPHTHQFL VWLPYDAEAL TEAAVRTAEE TGVALFRIWD HAGLPGIAHT EVLVEEPGLA
     WSTAEITAAV VDFLSRVR
//
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