ID Q5LKE6_RUEPO Unreviewed; 324 AA.
AC Q5LKE6;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Pyridoxal-phosphate dependent enzyme {ECO:0000313|EMBL:AAV97566.1};
GN OrderedLocusNames=SPOA0435 {ECO:0000313|EMBL:AAV97566.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OG Plasmid megaplasmid Spo {ECO:0000313|Proteomes:UP000001023}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV97566.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV97566.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RC PLASMID=Plasmid megaplasmid Spo {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV97566.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RC PLASMID=Plasmid megaplasmid Spo {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000032; AAV97566.1; -; Genomic_DNA.
DR RefSeq; WP_011242212.1; NC_006569.1.
DR AlphaFoldDB; Q5LKE6; -.
DR PaxDb; 246200-SPOA0435; -.
DR KEGG; sil:SPOA0435; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000001023; Plasmid megaplasmid Spo.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01562; Thr-dehyd; 1.
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; PTHR43050; SERINE / THREONINE RACEMASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43050:SF1; SERINE RACEMASE; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Plasmid {ECO:0000313|EMBL:AAV97566.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT DOMAIN 15..308
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 324 AA; 33727 MW; 6A0C1944A8D79BF1 CRC64;
MSTLELIEAA AERLSGHVRR TPLLSSPFLD EIAGRRVLVK PECLQHTGSF KFRGAWSAIS
ALDPEARARG VIAFSSGNHA QGVAHAATLH GIASVIVMPS DAPRLKIDNT RALGAEVVLY
DRGRESREEI GTALAGERGL TLIRPYDEPQ VIAGQASVGL ELAEQAGELG VESGDVLVCC
GGGGLTSGVA LALEARAPGL RARPVEPEGF DDVKRSLAGG TISRNNSETG NICDAILTPE
PGRITFPILS RLCGPGLAVT EDEALRAMAL AFLRLKIVLE PGGAVSLAAA LFHPDQVEGD
TVLAVASGGN VDAALFRTAL ELHA
//
