ID A0A0Q7Z6W5_9SPHN Unreviewed; 378 AA.
AC A0A0Q7Z6W5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KQZ64120.1};
GN ORFNames=ASD67_06300 {ECO:0000313|EMBL:KQZ64120.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ64120.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ64120.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ64120.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DSD1 family.
CC {ECO:0000256|ARBA:ARBA00005323}.
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:KQZ64120.1}.
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; LMGF01000003; KQZ64120.1; -; Genomic_DNA.
DR RefSeq; WP_056344862.1; NZ_LMGF01000003.1.
DR AlphaFoldDB; A0A0Q7Z6W5; -.
DR STRING; 1736474.ASD67_06300; -.
DR OrthoDB; 9772497at2; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR CDD; cd06819; PLPDE_III_LS_D-TA; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR Gene3D; 2.40.37.20; D-serine dehydratase-like domain; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR28004:SF2; D-SERINE DEHYDRATASE; 1.
DR PANTHER; PTHR28004; ZGC:162816-RELATED; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR Pfam; PF14031; D-ser_dehydrat; 1.
DR SMART; SM01119; D-ser_dehydrat; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
FT DOMAIN 271..361
FT /note="D-serine dehydratase-like"
FT /evidence="ECO:0000259|SMART:SM01119"
SQ SEQUENCE 378 AA; 39135 MW; 850BF701D49D051F CRC64;
MTDDLTLHAH LIGRQGSRAD LNTPVLVLDV DALDRNIAAM ASLAASHGVG LRPHAKTHKS
VDIAKRQLAA GAAGVCCAKI GEAEVLAAGG ITGLLITSPV AAPRAIERLA ALAKSAAGLM
AVVDHPAVAG RIDAALATSL DVVIDIDPGI ARTGVASPEA AVALAEAIAA LPNLRYRGVQ
YYCGSQQHIE GFADRRAAIE DRTAYLRTVI AALAHAGFPP EIVTGSGTGT HRIDLDLAIF
TELQAGSYVF MDKQYLDCDL TGDGTVPFET SLGVDARVVS ANHSGLVTID AGYKALSTDG
GVAVVRRGAP ETAFFAFMGD EHAALIAPGI GETLAPGDPV TLTVPHCDPT VNLYDHYHVV
ADETLVAIWP VSARGRAR
//