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Database: UniProt
Entry: F4C1A5_SPHS2
LinkDB: F4C1A5_SPHS2
Original site: F4C1A5_SPHS2 
ID   F4C1A5_SPHS2            Unreviewed;       340 AA.
AC   F4C1A5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ADZ78039.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:ADZ78039.1};
GN   OrderedLocusNames=Sph21_1477 {ECO:0000313|EMBL:ADZ78039.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78039.1};
RN   [1] {ECO:0000313|EMBL:ADZ78039.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ78039.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) 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; CP002584; ADZ78039.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C1A5; -.
DR   STRING; 743722.Sph21_1477; -.
DR   KEGG; shg:Sph21_1477; -.
DR   PATRIC; fig|743722.3.peg.1585; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_049619_0_0_10; -.
DR   OrthoDB; 9774495at2; -.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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; 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   Lyase {ECO:0000313|EMBL:ADZ78039.1}.
FT   DOMAIN          4..290
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   340 AA;  38418 MW;  24603E0F208523CB CRC64;
     MKSLASDNYA GAITEVMQAL LHENQDHAVA YGNDKTTERL KDELRLLINY QFKLHLVFNG
     TGANLLALSL LTKPYDAILC AETAHIYVDE STAPEGLTGC RLIPLPIDET GKLTPATIQR
     AVKRRGDLHH PQIKVLSITQ PTEYGTLYTL DELRGIHRVA NENDLLIHMD GSRLFTAITA
     LNCTLQDVVQ ASGVDALSLG GTKSGMLYGE AVLVFNEHIH DSPFFHKRSM QLASKSRFIS
     AQFLALLNHD TYRKYANIVL ERTQQLATVL RKYPQIIITK PVEVNAIFAK IPPNWIKPLQ
     ETLFFYLWDE HMHEVRLMCS FDTSEEEISL FDRKLAELTR
//
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