ID   D2RZJ5_HALTV            Unreviewed;       386 AA.
AC   D2RZJ5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent protein beta subunit {ECO:0000313|EMBL:ADB62034.1};
GN   OrderedLocusNames=Htur_3169 {ECO:0000313|EMBL:ADB62034.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62034.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB62034.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP001860; ADB62034.1; -; Genomic_DNA.
DR   RefSeq; WP_012944293.1; NC_013743.1.
DR   AlphaFoldDB; D2RZJ5; -.
DR   STRING; 543526.Htur_3169; -.
DR   GeneID; 8743789; -.
DR   KEGG; htu:Htur_3169; -.
DR   eggNOG; arCOG01434; Archaea.
DR   HOGENOM; CLU_028142_4_0_2; -.
DR   OrthoDB; 85597at2157; -.
DR   Proteomes; UP000001903; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
FT   DOMAIN          67..380
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   386 AA;  41426 MW;  EAE23AA5E8F65F5C CRC64;
     MASDLICPNC ETVYEAGPTE PWRCACGHAL EFTERPHPQG DPLPLQRLDT TEGLWTFFEF
     LPIEKHVTFH EGFTPLVDAP DWDAQFKLEY VFPTGSFKDR GATTTLSRAV ELGVERVIED
     SSGNAGAAIA TYAARAGLEA DIYVPADVKQ SKLMAIQRAD ARPVRVEGSR QDVTDACIDA
     VEGEARSASD EQSGDTPRQT GAGWYASHAW NPAFYAGTMT IAFEIAAQQG WTVPDAVVLP
     IGHGTLFLGA YRGFSLLNEA GIVDGMPRLL GAQATGYAPI VDELGGRRTE EDEDTDGADI
     ADGIRIAEPA RKDEILRAIE ETGGDAIALG ADPIETALDR LHRGGFYVEP TCAVAPAALE
     QYRDDDVLDA DADVVVPLTG SGLKTL
//