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Database: UniProt
Entry: K0KD42_SACES
LinkDB: K0KD42_SACES
Original site: K0KD42_SACES 
ID   K0KD42_SACES            Unreviewed;       289 AA.
AC   K0KD42;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Ectoine utilization protein {ECO:0000313|EMBL:CCH34478.1};
GN   OrderedLocusNames=BN6_72450 {ECO:0000313|EMBL:CCH34478.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH34478.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH34478.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; HE804045; CCH34478.1; -; Genomic_DNA.
DR   RefSeq; WP_015104589.1; NC_019673.1.
DR   AlphaFoldDB; K0KD42; -.
DR   STRING; 1179773.BN6_72450; -.
DR   KEGG; sesp:BN6_72450; -.
DR   PATRIC; fig|1179773.3.peg.7320; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_2_11; -.
DR   OrthoDB; 4408011at2; -.
DR   BioCyc; SESP1179773:BN6_RS34990-MONOMER; -.
DR   Proteomes; UP000006281; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT   DOMAIN          13..282
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   289 AA;  29520 MW;  1D13D9111F74B222 CRC64;
     MTSADVVAAA DRIRPHVRRT PLWRVEVDGR PLVLKLEHLQ LSGSFKLRGA VNTLLTADVP
     DRVVTASGGN HGLGVATAAR LLGTQATVYV PVSAPEGKVR RIEAAGAKLI RAGATYAQAV
     EAAREASGFY VEAYNDLAVI AGQGTVAAEV VEDAPDVDVV AVAVGGGGLA AGAALSGLHV
     AAVEPENCRA MHDALAAGEP VDSVVDSVAS SALGASRAGT VPFGILQAAG ASSVLVSDDE
     LLSARDRLWE EFRLAVEPAA AVPFAAWLHG RIPGTVCVVL CGANTDWTP
//
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