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Database: UniProt
Entry: S2XVV8_9ACTN
LinkDB: S2XVV8_9ACTN
Original site: S2XVV8_9ACTN 
ID   S2XVV8_9ACTN            Unreviewed;       416 AA.
AC   S2XVV8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=HMPREF1211_07584 {ECO:0000313|EMBL:EPD56463.1};
OS   Streptomyces sp. HGB0020.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD56463.1, ECO:0000313|Proteomes:UP000014410};
RN   [1] {ECO:0000313|EMBL:EPD56463.1, ECO:0000313|Proteomes:UP000014410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB0020 {ECO:0000313|EMBL:EPD56463.1,
RC   ECO:0000313|Proteomes:UP000014410};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptomyces sp. HGB0020.";
RL   Submitted (APR-2013) 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}.
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:EPD56463.1}.
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DR   EMBL; AGER01000030; EPD56463.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2XVV8; -.
DR   STRING; 1078086.HMPREF1211_07584; -.
DR   PATRIC; fig|1078086.3.peg.7639; -.
DR   HOGENOM; CLU_029381_4_0_11; -.
DR   Proteomes; UP000014410; 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:UP000014410}.
FT   DOMAIN          85..312
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  45398 MW;  5ABFB103A09952CB CRC64;
     MIRTMSDAAE QGGRTAGQLS DAGQLSDEER LKQRRKRRIS AYRSASRVLA RPGFLGTLRE
     RLALLDDAQH FYDLDEPSDI YGNGVVAALE EKVAHLLGKE AAAFFPTGTM AQQVALRCWA
     GRTGSPAVAL HALAHPEVHE RHAFSQVSGL RPVRVTGESR FLTADEVREF DEPFGTLMLE
     LPLRDAGFVL PSWEELTAVV EAARERDAVV HFDGARLWES TTHFGRPLDE IADLADTVYV
     SFYKSLDGYG GAALAGPKTL VDEAKVWRHR YGGQIFQQFP TALSALAGLE RELPRLPAYV
     AHARVVAEAL REGFAATGVP WTIVHPEVPH TNEFQLWLPH DVDVVSEAAI RQGEETGVLL
     FADAWDAKGP GLAMTEVSVR AAGLEWTADD VKAAVAQFAS RLTEEADRAK AAGGGR
//
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