ID   A0A0X8HCC3_9GAMM        Unreviewed;       414 AA.
AC   A0A0X8HCC3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=D-threonine aldolase {ECO:0000313|EMBL:AMD00042.1};
DE            EC=4.1.2.42 {ECO:0000313|EMBL:AMD00042.1};
GN   ORFNames=LOKO_00965 {ECO:0000313|EMBL:AMD00042.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD00042.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMD00042.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00042.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT   Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMD00042.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00042.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DSD1 family.
CC       {ECO:0000256|ARBA:ARBA00005323}.
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DR   EMBL; CP014226; AMD00042.1; -; Genomic_DNA.
DR   RefSeq; WP_066445769.1; NZ_CP014226.1.
DR   AlphaFoldDB; A0A0X8HCC3; -.
DR   STRING; 507626.LOKO_00965; -.
DR   KEGG; hco:LOKO_00965; -.
DR   PATRIC; fig|507626.3.peg.954; -.
DR   OrthoDB; 9811417at2; -.
DR   Proteomes; UP000063387; Chromosome.
DR   GO; GO:0043876; F:D-threonine aldolase activity; IEA:UniProtKB-EC.
DR   CDD; cd06818; PLPDE_III_cryptic_DSD; 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:SF8; D-SERINE DEAMINASE; 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;
KW   Lyase {ECO:0000313|EMBL:AMD00042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387}.
FT   DOMAIN          295..401
FT                   /note="D-serine dehydratase-like"
FT                   /evidence="ECO:0000259|SMART:SM01119"
SQ   SEQUENCE   414 AA;  45189 MW;  F6CF8CD37EB79867 CRC64;
     MIEPNSRHPD ATSLHKGLPE TGNRLLADVS LPAAVIHEAA LAHNLAWMQR FCEAHGARLA
     PHGKTTMTPA LFHRQLQAGA WGITLATAAQ CRAAFAHGVR RLLMANQLVG EANMAIVAGL
     IEAGADFYCV VDSAENVRQL GRYFAARGLC LQVLIELGVD GARCGCRGQN EVMALGELVE
     SEQALVLSGL EGFEGVVHGD DQESQVRGYA WQLVEAAQAL DHDGLIENPH PLITASGSVW
     YDLVAEVFLE AGLGSHFVPV LRPGCYVVHD HGIYRSAQHA VLGRRPGIDQ GLRPALEVYA
     QVVSLPEPGL AILGLGKRDI GHDQMPEPLR RHREGGSIGD IRSVAGWRIT KLMDQHAFVT
     LPHDERDEPR HDPVRVGDIV ALGISHPCLT FDKWRRLCRV DERLEVIEVM ETCF
//