ID A0A0H2KLM8_9MICO Unreviewed; 436 AA.
AC A0A0H2KLM8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=FB00_12625 {ECO:0000313|EMBL:KLN34391.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN34391.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN34391.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN34391.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-2014) 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:KLN34391.1}.
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DR EMBL; JNBQ01000015; KLN34391.1; -; Genomic_DNA.
DR RefSeq; WP_047233220.1; NZ_JNBQ01000015.1.
DR AlphaFoldDB; A0A0H2KLM8; -.
DR STRING; 264251.FB00_12625; -.
DR PATRIC; fig|264251.5.peg.2571; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000035265; 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:UP000035265};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 88..423
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 436 AA; 46202 MW; A339DDA0950B8A8C CRC64;
MTTQQSPVPV RSLEPTGAEV PSTVPTHWYN LAADLPEPVP PHLHPGTREP LTPDDLAPLF
PLALVQQEVT TERYVEIPQT IREIYALWRP SPLVRARRLE RALGTPARIY YKYEGVSPVG
SHKPNTAVAQ AYYNALEGTT KLTTETGAGQ WGASLSFAGA LLGLDVEVWQ VRASYDSKPY
RRAQMEVYGG ICHPSPSDLT EAGRAMLAAD PETTGSLGMA ISEAVETAAK DPAAHYALGS
VLNHVMLHQS VIGQEALVQL DEAGEGAPDV VFGCAGGGSN LAGLTFPFLG RNLREGTTTR
LVACEPAACP SLTQGEYRYD FGDVAGLTPL LKMHTLGKDF VPPAIHAGGL RYHGMSPMVS
HAVNLGLMDA IAVDQDEAFT AGTLFARSEG IIPAPESTHA VAAAVAHARA ATEPEVIVLG
LSGNGVLDLP AYASYV
//
