ID A0A2Z2HKI4_9ARCH Unreviewed; 396 AA.
AC A0A2Z2HKI4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=trpB1 {ECO:0000313|EMBL:ARS64504.1};
GN Synonyms=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=NMSP_0885 {ECO:0000313|EMBL:ARS64504.1};
OS Candidatus Nitrosomarinus catalina.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosomarinus.
OX NCBI_TaxID=1898749 {ECO:0000313|EMBL:ARS64504.1, ECO:0000313|Proteomes:UP000249949};
RN [1] {ECO:0000313|EMBL:ARS64504.1, ECO:0000313|Proteomes:UP000249949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPOT01 {ECO:0000313|EMBL:ARS64504.1,
RC ECO:0000313|Proteomes:UP000249949};
RX PubMed=28418097;
RA Ahlgren N.A., Chen Y., Needham D.M., Parada A.E., Sachdeva R., Trinh V.,
RA Chen T., Fuhrman J.A.;
RT "Genome and epigenome of a novel marine Thaumarchaeota strain suggest viral
RT infection, phosphorothioation DNA modification and multiple restriction
RT systems.";
RL Environ. Microbiol. 19:2434-2452(2017).
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; CP021324; ARS64504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2HKI4; -.
DR KEGG; nct:NMSP_0885; -.
DR OrthoDB; 371827at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000249949; Chromosome.
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 53..377
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 88
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 396 AA; 43370 MW; 087C42C94E221C9C CRC64;
MKYPKNGKFG EFGGQYIPET LVPAIEELEE NYLKFKNDKK FKQELDYYLK VYAGRPTPLY
YAKNLSEKLG GGKIYLKRED LLHGGAHKIN NTLGQALLAK KMNKKRIIAE TGAGQHGVAT
AMACAALGMK AEVYMGYKDT IRQKQNVYRM NMLGSKVHPV KSGSKTLKDA INDAIRDWIT
NVESTYYLLG SAVGPHPYPV MVRDFQSVIG NEIKSQMKKI NNKEPDTVIA CVGGGSNAIG
TFYPLVDTSA EIIGVEAAGM GLKSKLHSAT LSAGSKGVLH GMMTYLLQDS EGQITETHSI
SAGLDYPGVG PEHAYYKDTK RVKYHSSTDK EVLDAFLILT QTEGIIPALE SSHAISEAMK
VAKKSKPSES IVVTLSGRGD KDVEEVQKYL DASKNN
//
