ID E1ICF6_9CHLR Unreviewed; 452 AA.
AC E1ICF6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=OSCT_1007 {ECO:0000313|EMBL:EFO81151.1};
OS Oscillochloris trichoides DG-6.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Oscillochloris.
OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO81151.1, ECO:0000313|Proteomes:UP000054010};
RN [1] {ECO:0000313|EMBL:EFO81151.1, ECO:0000313|Proteomes:UP000054010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO81151.1,
RC ECO:0000313|Proteomes:UP000054010};
RX PubMed=21037015; DOI=10.1128/JB.00931-10;
RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT Oscillochloris trichoides subsp. DG-6.";
RL J. Bacteriol. 193:321-322(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO81151.1}.
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DR EMBL; ADVR01000024; EFO81151.1; -; Genomic_DNA.
DR RefSeq; WP_006561567.1; NZ_GL501402.1.
DR AlphaFoldDB; E1ICF6; -.
DR STRING; 765420.OSCT_1007; -.
DR eggNOG; COG1350; Bacteria.
DR HOGENOM; CLU_042858_1_0_0; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000054010; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR006316; Trp_synth_b-like.
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; TIGR01415; trpB_rel; 1.
DR PANTHER; PTHR48077:SF6; TRYPTOPHAN SYNTHASE BETA CHAIN; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR PIRSF; PIRSF500824; TrpB_prok; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054010};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 76..414
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 452 AA; 48817 MW; F5B642E3FE9434AE CRC64;
MNTIKYLLDE DKMPTHWYNV AADLPTPAAP ALHPGTGQPL GPADLAPLFP MALIMQEVST
ERSIEIPDEV QQIYRQWRPS PLFRARRLEK ALDTPAKIYY KYEGVSPAGS HKPNTAIAQA
YYNKIEGTKR LVTETGAGQW GSSLAFAGAL FGLEVEIYMV KVSYNQKPYR RALMEVYGAR
VVASPSTETA CGRAILAEHP DSTGSLGIAI SEAVEMAVQR DDTKYALGSV LNHVMLHQTV
IGEEAIAQME MAGDYPDVIV GCTGGGSNFA GLTFPFIGAK LRGERDVRVI AVEPAACPTL
TKGKFTYDFG DTAHLTPLVK MHTLGSTFVP SGIHAGGLRY HGMGPLVSHL LDLGTIDAVA
VQQLETFSAG LQFARTEGIL PAPESNHAVA ATIREALRCK EEGKSETILF NLSGHGHFDL
QAYMDFQAGT LKDFEYSDEE VAMALAGLPS VG
//
