ID Q0ABV5_ALKEH Unreviewed; 451 AA.
AC Q0ABV5;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
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 OrderedLocusNames=Mlg_0327 {ECO:0000313|EMBL:ABI55682.1};
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI55682.1, ECO:0000313|Proteomes:UP000001962};
RN [1] {ECO:0000313|Proteomes:UP000001962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC {ECO:0000313|Proteomes:UP000001962};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000453; ABI55682.1; -; Genomic_DNA.
DR RefSeq; WP_011628078.1; NC_008340.1.
DR AlphaFoldDB; Q0ABV5; -.
DR KEGG; aeh:Mlg_0327; -.
DR eggNOG; COG1350; Bacteria.
DR HOGENOM; CLU_042858_1_0_6; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001962; Chromosome.
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:UP000001962};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 75..412
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 451 AA; 49089 MW; A4831E9FE7B0B91F CRC64;
MSDTKIYLPE SDIPRHWYNV IPDMPTPPQP YLGPDGKPIT GAAMEAIFPP AIIEQETSSE
RWIPIPEPVR EALTLWRPSP LIRARRLEQA LNTPAKIYFK YEGVSPAGSH KPNSAVAQAY
YNAEAGIKRL TTETGAGQWG SSLALAGQMF GLDVRIYMVR ISYEQKPYRR SMMETWGGEV
IPSPSNHTQA GRDALAQDPD SNGSLGMAIS EAVEEAASRG DTNYALGSVL NHVLLHQTVI
GLEAKRQMEI AGDYPDVVFA PCGGGSNVGG IMFPFLADKA AGRDLRLVAV EPASCPTLTR
GHFAYDYGDS VGLTPMMKMY TLGHDFMPPG IHAGGLRYHG DSALVSQLYH DGVLEARSVH
QTATFQAGVL FARTQGIIPA PESAHAIRAA VDEAVQAREE GRERTILFTL SGHGHFDMSA
YDRYFAGELE DMDYPTEALE TAKANLPKVE G
//
