O06739 (PSLS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphosulfolactate synthase
EC=4.4.1.19

Alternative name(s):
(2R)-phospho-3-sulfolactate synthase
Short name=PSL synthase

Gene names

Name:	yitD
Ordered Locus Names:	BSU10950

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL) By similarity. Is probably involved in the biosynthesis of L-sulfolactate, which is a major constituent of sporulating cells and mature spores. Ref.3
Catalytic activity	(2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + hydrogen sulfite.
Sequence similarities	Belongs to the phosphosulfolactate synthase family.

Ontologies

Keywords
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	coenzyme M biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	phosphosulfolactate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 252

252

Phosphosulfolactate synthase

PRO_0000080832

Secondary structure

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252

Helix Strand Turn

Details...

Beta strand

17 – 19

3

Beta strand

21 – 27

7

Helix

30 – 40

11

Helix

41 – 43

3

Beta strand

46 – 49

4

Helix

53 – 56

4

Helix

60 – 69

10

Beta strand

73 – 76

4

Helix

78 – 86

9

Helix

90 – 99

10

Beta strand

103 – 107

5

Beta strand

110 – 112

3

Helix

116 – 126

11

Turn

127 – 129

3

Beta strand

130 – 135

6

Helix

151 – 162

12

Beta strand

164 – 169

6

Helix

191 – 195

5

Turn

196 – 198

3

Helix

201 – 203

3

Beta strand

204 – 207

4

Helix

211 – 221

11

Beta strand

227 – 231

5

Helix

232 – 234

3

Helix

235 – 242

8

Helix

247 – 249

3

Sequences

	Sequence		Length	Mass (Da)
	O06739 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 7904A18AF982C970	FASTA	252	28,357
	10 20 30 40 50 60 MNDFSLELPV RTNKPRETGQ SILIDNGYPL QFFKDAIAGA SDYIDFVKFG WGTSLLTKDL 70 80 90 100 110 120 EEKISTLKEH DITFFFGGTL FEKYVSQKKV NEFHRYCTYF GCEYIEISNG TLPMTNKEKA 130 140 150 160 170 180 AYIADFSDEF LVLSEVGSKD AELASRQSSE EWLEYIVEDM EAGAEKVITE ARESGTGGIC 190 200 210 220 230 240 SSSGDVRFQI VDDIISSDID INRLIFEAPN KTLQQGFIQK IGPNVNLANI PFHDAIALET 250 LRLGLRSDTF FL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees position encoding 11 membrane proteins." Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J. Microbiology 143:3309-3312(1997) [PubMed: 9353932] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis in Xanthobacter strain Py2." Krum J.G., Ensign S.A. J. Bacteriol. 183:2172-2177(2001) [PubMed: 11244054] [Abstract] Cited for: PROBABLE FUNCTION.
[4]	"PSL synthase from Bacillus subtilis." Midwest center for structural genomics (MCSG) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y09476 Genomic DNA. Translation: CAA70659.1.
AL009126 Genomic DNA. Translation: CAB12935.1.

PIR

E69839.

RefSeq

NP_388976.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U83	X-ray	2.20	A	1-252	[»]

ProteinModelPortal

O06739.

SMR

O06739. Positions 3-251.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003014; EBBACP00000003014; EBBACG00000003008.

GeneID

939794.

GenomeReviews

Gene locus BSU10950 in contig AL009126_GR.

KEGG

bsu:BSU10950.

NMPDR

fig|224308.1.peg.1095.

PATRIC

18973896. VBIBacSub10457_1142.

Organism-specific databases

GenoList

BSU10950.

Phylogenomic databases

GeneTree

EBGT00050000006604.

HOGENOM

HBG363100.

OMA

GGTLFEK.

PhylomeDB

O06739.

ProtClustDB

CLSK887042.

Enzyme and pathway databases

BioCyc

BSUB:BSU10950-MONOMER.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR003830. ComA_synth.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K08097.

Pfam

PF02679. ComA. 1 hit.
[Graphical view]

SUPFAM

SSF102110. ComA_synth. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PSLS_BACSU

Accession

Primary (citable) accession number: O06739

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program