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Database: UniProt
Entry: F2JZZ5_MARM1
LinkDB: F2JZZ5_MARM1
Original site: F2JZZ5_MARM1 
ID   F2JZZ5_MARM1            Unreviewed;       421 AA.
AC   F2JZZ5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=Marme_2885 {ECO:0000313|EMBL:ADZ92107.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ92107.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ92107.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
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; CP002583; ADZ92107.1; -; Genomic_DNA.
DR   RefSeq; WP_013662010.1; NZ_CP047696.1.
DR   AlphaFoldDB; F2JZZ5; -.
DR   STRING; 717774.Marme_2885; -.
DR   KEGG; mme:Marme_2885; -.
DR   PATRIC; fig|717774.3.peg.2972; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_6; -.
DR   OMA; GPEHAMF; -.
DR   OrthoDB; 9766131at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001062; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00133}.
FT   DOMAIN          53..379
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         87
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   421 AA;  46037 MW;  F4E76C75A33F0C90 CRC64;
     MQSDNGYYGE FGGSYIPEIL YSSQQQILNA YEEAKNDPAF IAELKQQWQE YSGRPTPLTF
     CKNLTEHFGG AQIYLKREDL NHSGAHKMNN VIGQGLLVKR MGKKRVIAET GAGQHGIATA
     LVCARLGLEC TIYMGAKDVK RQYPNVFWME QLGATVVPVT EGSQTLRDAL DEALRDWSST
     HEDSHYLIGT TCGCAPFPEM VAFFQSVIGE EVKEQSKAQF GRYPDKLYAC VGGGSNACGL
     FLPFVDDKDV EMVGVEAGGK GTKLGEHSIR LSHNLGTPGI AQGFASIFIQ DDAGQLQETH
     SISAGLDYVG VSPIIAHLAK EGRINMTYAM DDEVVDACTL LLKNEGIIPA LESSHALAGA
     FKDAPSMSKD THIVINLSGR GDKDIFNVAK ALQDPTFPNF LNDYLEDYEK DTLIKKTEKE
     A
//
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