ID A0A0Q9CK46_9CELL Unreviewed; 446 AA.
AC A0A0Q9CK46;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ASE27_05070 {ECO:0000313|EMBL:KRD40305.1};
OS Oerskovia sp. Root918.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Oerskovia.
OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40305.1, ECO:0000313|Proteomes:UP000051694};
RN [1] {ECO:0000313|EMBL:KRD40305.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40305.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD40305.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40305.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRD40305.1}.
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DR EMBL; LMJG01000011; KRD40305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9CK46; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000051694; 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 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; 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:UP000051694};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 98..433
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 446 AA; 47494 MW; 6C30F7066663F55C CRC64;
MTTSPVSTPA APSAPATPTA RSLEPLGVEI PSTVPTHWYN LNADLPEPVP PHLHPGTLEP
LVPEDLAPLF PMALIEQEVS TERYIEIPQT IREIYAMWRP APLIRAHRLE RELGTPARIY
YKYEGVSPVG SHKPNTAIAQ AYYNAIEGTT RLTTETGAGQ WGASLSMAAA LLGLTCEVWQ
VRASYDSKPY RRFQMEAYGG VCHSSPSELT ASGRAILASD PDTTGSLGMA ISEAVEVAAQ
DPQAHYSLGS VLNHVMLHQT VIGQEALVQL EEAGETGADV VFGCAGGGSN LAGLTFPFLG
RNLREGTTTR LVACEPAACP SLTQGEYRYD HGDVVGLTPL LKMHTLGKDF VPPAIHAGGL
RYHGMSPMVS HAVNLGLMDA VAIDQDEAFR AGLEFARSEG IIPAPESTHA VAAAIAYART
VTEPEVVVIG LSGNGQLDLP AYAQYV
//
