ID Q9LAG9_AZOBR Unreviewed; 405 AA.
AC Q9LAG9;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 113.
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 ECO:0000313|EMBL:AAF61457.1};
GN ORFNames=D2T81_24415 {ECO:0000313|EMBL:RIV99070.1}, D3093_08450
GN {ECO:0000313|EMBL:QCN95280.1}, D3867_10700
GN {ECO:0000313|EMBL:QCO02437.1}, D3868_09700
GN {ECO:0000313|EMBL:QCO09281.1}, D3869_06735
GN {ECO:0000313|EMBL:QCO14941.1}, DS837_09270
GN {ECO:0000313|EMBL:KAA0686636.1}, FH063_000022
GN {ECO:0000313|EMBL:KAA1057822.1};
OS Azospirillum brasilense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192 {ECO:0000313|EMBL:AAF61457.1};
RN [1] {ECO:0000313|EMBL:AAF61457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sp7 {ECO:0000313|EMBL:AAF61457.1};
RX PubMed=11092742;
RA Dosselaere F., Lambrecht M., Vanderleyden J.;
RT "Isolation and sequence analysis of the trpBA gene cluster, encoding
RT tryptophan synthase, from Azospirillum brasilense.";
RL DNA Seq. 11:287-293(2000).
RN [2] {ECO:0000313|EMBL:KAA0686636.1, ECO:0000313|Proteomes:UP000476837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49958 {ECO:0000313|EMBL:KAA0686636.1,
RC ECO:0000313|Proteomes:UP000476837};
RA Sant'Anna F.H., Baldani J.I., Zilli J.E., Reis V.M., Hartmann A., Cruz L.,
RA de Souza E.M., de Oliveira Pedrosa F., Passaglia L.M.P.;
RT "Genome sequence of Roseomonas fauriae ATCC 49958.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RIV99070.1, ECO:0000313|Proteomes:UP000283844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR80 {ECO:0000313|EMBL:RIV99070.1,
RC ECO:0000313|Proteomes:UP000283844};
RA Gogoleva N.E., Burygin G.L., Shagimardanova E.I., Gogolev Y.V.;
RT "Genome Data for Oil-Degrading Strain Azospirillum brasilense SR80, a
RT Rhizospheric Bacterium Isolated from Wheat.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000298595, ECO:0000313|Proteomes:UP000298596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC4035 {ECO:0000313|EMBL:QCN95280.1,
RC ECO:0000313|Proteomes:UP000298595}, MTCC4036
RC {ECO:0000313|EMBL:QCO02437.1, ECO:0000313|Proteomes:UP000298596},
RC MTCC4038 {ECO:0000313|EMBL:QCO09281.1,
RC ECO:0000313|Proteomes:UP000298774}, and MTCC4039
RC {ECO:0000313|EMBL:QCO14941.1, ECO:0000313|Proteomes:UP000298693};
RA Singh C., Tripathi A.K.;
RT "Whole genome based analysis of evolution and adaptive divergence in Indian
RT and Brazilian strains of Azospirillum brasilense.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:KAA1057822.1, ECO:0000313|Proteomes:UP000325333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Az19 {ECO:0000313|EMBL:KAA1057822.1,
RC ECO:0000313|Proteomes:UP000325333};
RA Maroniche G.A., Garcia J.E., Pagnussat L., Amenta M., Creus C.M.;
RT "Genome sequencing of the stress-tolerant strain Azospirillum brasilense
RT Az19.";
RL Submitted (JUL-2019) 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|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; AF139661; AAF61457.1; -; Genomic_DNA.
DR EMBL; QOKV01000004; KAA0686636.1; -; Genomic_DNA.
DR EMBL; VEWN01000001; KAA1057822.1; -; Genomic_DNA.
DR EMBL; CP032321; QCN95280.1; -; Genomic_DNA.
DR EMBL; CP032330; QCO02437.1; -; Genomic_DNA.
DR EMBL; CP032339; QCO09281.1; -; Genomic_DNA.
DR EMBL; CP032345; QCO14941.1; -; Genomic_DNA.
DR EMBL; QXHE01000071; RIV99070.1; -; Genomic_DNA.
DR RefSeq; WP_014238652.1; NZ_WFKD01000225.1.
DR GeneID; 56450017; -.
DR KEGG; aare:D3093_08450; -.
DR KEGG; abf:AMK58_01630; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000283844; Unassembled WGS sequence.
DR Proteomes; UP000298595; Chromosome.
DR Proteomes; UP000298596; Chromosome.
DR Proteomes; UP000298693; Chromosome.
DR Proteomes; UP000298774; Chromosome.
DR Proteomes; UP000325333; Unassembled WGS sequence.
DR Proteomes; UP000476837; Unassembled WGS sequence.
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 62..388
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 405 AA; 44098 MW; DAB89EBB7CEC4DF8 CRC64;
MTRPNTYRSG PDERGHFGIY GGRFVAETLM PLILEVEKAY REARADPAFE GAIREQLKQY
VGRPNPLYYA ERLTEKLGGA KIYFKREELN HTGAHKINNC IGQILLARRM GKKRIIAETG
AGQHGVATAT VCALFDMPCV IYMGETDIAR QQPNVFRMKL LGAEVVPVTS GARTLKDAMN
EALRDWVTNV ADTYYLIGTA AGPHPYPAMV RDFQSVIGDE VRVQMQELEG RLPDSLVACV
GGGSNAIGLF HPFLDDPSVQ MVAVEAAGHG IDKGPLAHAA SITGGRPGVL HGNRTYLLQD
EDGQILEGHS ISAGLDYPGV GPEHSWLHDI GRVEYVSATD QETLDAFQLC ARTEGIIPAL
ESAHALAEIV KRAPKLPKDH LMVLCLSGRG DKDIFSVAQH LGVKL
//
