PSLS_BACSU
ID PSLS_BACSU Reviewed; 252 AA.
AC O06739;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphosulfolactate synthase;
DE EC=4.4.1.19;
DE AltName: Full=(2R)-phospho-3-sulfolactate synthase;
DE Short=PSL synthase;
GN Name=yitD; OrderedLocusNames=BSU10950;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT position encoding 11 membrane proteins.";
RL Microbiology 143:3309-3312(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROBABLE FUNCTION.
RX PubMed=11244054; DOI=10.1128/jb.183.7.2172-2177.2001;
RA Krum J.G., Ensign S.A.;
RT "Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and
RT epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis
RT in Xanthobacter strain Py2.";
RL J. Bacteriol. 183:2172-2177(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "PSL synthase from Bacillus subtilis.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the addition of sulfite to phosphoenolpyruvate
CC (PEP) to yield (2R)-phospho-3-sulfolactate (PSL) (By similarity). Is
CC probably involved in the biosynthesis of L-sulfolactate, which is a
CC major constituent of sporulating cells and mature spores.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-O-phospho-3-sulfolactate = H(+) + phosphoenolpyruvate +
CC sulfite; Xref=Rhea:RHEA:22784, ChEBI:CHEBI:15378, ChEBI:CHEBI:15597,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:58702; EC=4.4.1.19;
CC -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family.
CC {ECO:0000305}.
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DR EMBL; Y09476; CAA70659.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12935.1; -; Genomic_DNA.
DR PIR; E69839; E69839.
DR RefSeq; NP_388976.1; NC_000964.3.
DR RefSeq; WP_003233048.1; NZ_JNCM01000035.1.
DR PDB; 1U83; X-ray; 2.20 A; A=1-252.
DR PDBsum; 1U83; -.
DR AlphaFoldDB; O06739; -.
DR SMR; O06739; -.
DR STRING; 224308.BSU10950; -.
DR PaxDb; O06739; -.
DR PRIDE; O06739; -.
DR EnsemblBacteria; CAB12935; CAB12935; BSU_10950.
DR GeneID; 939794; -.
DR KEGG; bsu:BSU10950; -.
DR PATRIC; fig|224308.179.peg.1177; -.
DR eggNOG; COG1809; Bacteria.
DR InParanoid; O06739; -.
DR OMA; SGICREN; -.
DR PhylomeDB; O06739; -.
DR BioCyc; BSUB:BSU10950-MON; -.
DR EvolutionaryTrace; O06739; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043817; F:phosphosulfolactate synthase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003830; ComA_synth.
DR InterPro; IPR036112; ComA_synth_sf.
DR Pfam; PF02679; ComA; 1.
DR SUPFAM; SSF102110; SSF102110; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..252
FT /note="Phosphosulfolactate synthase"
FT /id="PRO_0000080832"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1U83"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1U83"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:1U83"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:1U83"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1U83"
SQ SEQUENCE 252 AA; 28357 MW; 7904A18AF982C970 CRC64;
MNDFSLELPV RTNKPRETGQ SILIDNGYPL QFFKDAIAGA SDYIDFVKFG WGTSLLTKDL
EEKISTLKEH DITFFFGGTL FEKYVSQKKV NEFHRYCTYF GCEYIEISNG TLPMTNKEKA
AYIADFSDEF LVLSEVGSKD AELASRQSSE EWLEYIVEDM EAGAEKVITE ARESGTGGIC
SSSGDVRFQI VDDIISSDID INRLIFEAPN KTLQQGFIQK IGPNVNLANI PFHDAIALET
LRLGLRSDTF FL
