ID D9XC37_STRVT Unreviewed; 356 AA.
AC D9XC37;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:EFL30268.1};
GN ORFNames=SSQG_00786 {ECO:0000313|EMBL:EFL30268.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL30268.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) 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; GG657757; EFL30268.1; -; Genomic_DNA.
DR RefSeq; WP_003988383.1; NZ_GG657757.1.
DR AlphaFoldDB; D9XC37; -.
DR STRING; 591159.SSQG_00786; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_0_0_11; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000004184; 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 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 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:UP000004184}.
FT DOMAIN 19..305
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 356 AA; 38978 MW; E346EFFF967DF461 CRC64;
MNPPKTDARR HHDPEVRGFA SDNYAGAHPE VLAALALANG GHQVAYGEDE YTDHLQGLVR
SHFGPTAEAF PVFNGTGANV VALQAVTDRW GAVICAESAH INVDECGAPE RVGGLKLLTV
PTPDGKLTPE LIDRQAYGWD DEHRAMPQVV SLAQATELGT LYTPDEIRTL CEHAHAHGMK
VHLDGSRLAN AAATLNVPMR TLTNAAGVDI LSLGGTKNGA LFGEAVVVID QDAVSHMKHL
RKLSMQLASK MRFVSVQLEA LLARDLWLRN ARHANEMAQR LAEGVRAVHG VEILYPVQAN
AVFARLPHDV SERLQKRFRF YFWDEAAGDV RWMCAFDTTE EDVDAFVAAL KEEMAR
//
