ID F7PLA8_9EURY Unreviewed; 387 AA.
AC F7PLA8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN Name=trpB1 {ECO:0000313|EMBL:ERJ05199.1};
GN Synonyms=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=HLRTI_002827 {ECO:0000313|EMBL:ERJ05199.1}, HTIA_2627
GN {ECO:0000313|EMBL:CCQ34732.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ05199.1, ECO:0000313|Proteomes:UP000003861};
RN [1] {ECO:0000313|EMBL:ERJ05199.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05199.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ05199.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05199.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ34732.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ34732.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000256|ARBA:ARBA00002786,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC Rule:MF_00133};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
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DR EMBL; HF571520; CCQ34732.1; -; Genomic_DNA.
DR EMBL; AFNT02000041; ERJ05199.1; -; Genomic_DNA.
DR RefSeq; WP_008526750.1; NZ_AFNT02000041.1.
DR STRING; 1033806.HTIA_2627; -.
DR GeneID; 23798830; -.
DR KEGG; hti:HTIA_2627; -.
DR PATRIC; fig|1033806.12.peg.2615; -.
DR eggNOG; arCOG01433; Archaea.
DR HOGENOM; CLU_016734_3_1_2; -.
DR OrthoDB; 371827at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 55..371
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 89
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 387 AA; 41593 MW; E4BC2FC8D2AFACAB CRC64;
MSNDSDDPGA FGDYGGRHVP DPLKEPLAQL AAAFEDVALS DEFQAEFRTL LEHYAGRPTP
LYHAERLSEA YGAEIYLKRE DLLHGGAHKL NNTLGQALLA KKAGKERLIA ETGAGQHGTA
TAMVGAMLDL DTEIYMGEKD VARQRMNVFR MRLMGAEVKE VSRGGKGLAD AVDAALEDFA
KNVEDTHYLV GSVVGPDPFP RMVREFQSVI GDEAREQIRD RIGGLPDAAV ACVGGGSNAI
GLFDAFRDDD VAFYGAEGGG EGADSNRHAA PLADGEDDVL HGMKTRVIDE ETEVHSVSAG
LDYPGVGPEH AMFRAVGRCD YRGITDEQAL EAFRELSMLE GIIPALETSH GLALAKQIAD
EHDTILVNLS GRGDKDMETA AEHFDLG
//
