ID A0A1E7JXV5_9ACTN Unreviewed; 368 AA.
AC A0A1E7JXV5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OEU96517.1};
GN ORFNames=AN216_19710 {ECO:0000313|EMBL:OEU96517.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU96517.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEU96517.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU96517.1,
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:OEU96517.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJGU01000137; OEU96517.1; -; Genomic_DNA.
DR RefSeq; WP_070198014.1; NZ_LJGU01000137.1.
DR AlphaFoldDB; A0A1E7JXV5; -.
DR STRING; 1075402.AN216_19710; -.
DR PATRIC; fig|1075402.3.peg.1416; -.
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 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:UP000176101}.
FT DOMAIN 27..313
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40033 MW; C348A703B00EA595 CRC64;
MAHTPAVASA PAVTDAKRHH DPEIRGFASD NYAGAHPEVL AALALANGGH QSAYGADAYT
EHLQQAMRSH FGPYAQAFPV FNGTGANVVA LQALTDRWGA VIAADSAHIH VDECGAPERV
GGLKLLTVPT ADGKLTPELI DREAFGWDDE HRAMPQVVSL AQNTELGTLY TPDEVRAICE
HAHERGMRVH LDGARIANAA AALDVPMRAF THAVGVDVLS FGGTKNGMLF GEAVVVLNPD
AVGAMKHLRK LSMQLASKAR FISVQLEALL ARDLWLRNAR HANTMAQRLA AGVRSVEGVR
ILYPVQANAV FARLPHEVSE RLQKRYRFYF WDEAAGDVRW MCSFDTTEED VDGFVSALRE
EMTESTHT
//
