STRINGSTRING
ilvA ilvA cysM cysM trpB trpB thrC thrC RB4386 RB4386 cysK cysK
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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ilvAThreonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (415 aa)
cysMCysteine synthase B; PMID: 2188958 best DB hits: BLAST: swissprot:P16703; CYSM_ECOLI CYSTEINE SYNTHASE B (O-ACETYLSERINE; E=1e-30 pir:D82758; cysteine synthase XF0831 [imported] - Xylella fastidiosa; E=1e-30 swissprot:P95230; CYSK_MYCTU CYSTEINE SYNTHASE A (O-ACETYLSERINE; E=2e-30 COG: cysM; COG0031 Cysteine synthase; E=1e-31 PFAM: PF00291; Pyridoxal-phosphate dependent enzyme; E=5.9e-51. (323 aa)
trpBTryptophan synthase beta chain 1; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (407 aa)
thrCThreonine synthase precursor; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (456 aa)
RB4386Cysteine synthase; PMID: 93345669 best DB hits: BLAST: swissprot:Q44004; CYSM_ALCEU CYSTEINE SYNTHASE (O-ACETYLSERINE; E=2e-35 pir:T43792; cysteine synthase (EC 4.2.99.8) cysK [similarity] -; E=1e-31 pir:H81161; probable cysteine synthase (EC 4.2.99.8) NMA0974; E=3e-31 COG: NMB0763; COG0031 Cysteine synthase; E=2e-32 PFAM: PF00291; Pyridoxal-phosphate dependent enzyme; E=9.2e-57. (349 aa)
cysKCysteine synthase (O-acetylserine sulfhydrylase); PMID: 10930739 best DB hits: BLAST: gb:AAG01804.1; AF276772_3 (AF276772) O-acetylserine sulfhydrylase; E=3e-83 swissprot:P95230; CYSK_MYCTU CYSTEINE SYNTHASE A (O-ACETYLSERINE; E=1e-82 pir:H81161; probable cysteine synthase (EC 4.2.99.8) NMA0974; E=1e-81 COG: Rv2334; COG0031 Cysteine synthase; E=1e-83 PFAM: PF00291; Pyridoxal-phosphate dependent enzym; E=1.3e-119. (319 aa)
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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