Cysteine synthase - Haemophilus influenzae

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Reviewed, UniProtKB/Swiss-Prot P45040 (CYSK_HAEIN)

Last modified February 9, 2010. Version 79. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cysteine synthase
      Short name=CSase
    EC=2.5.1.47
Alternative name(s):
    O-acetylserine sulfhydrylase
    O-acetylserine (thiol)-lyase
      Short name=OAS-TL

Gene names

Name:	cysK
Ordered Locus Names:	HI1103

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	O(3)-acetyl-L-serine + H₂S = L-cysteine + acetate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro
Molecular function	cysteine synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

Cysteine synthase

PRO_0000167090

Regions

Region

177 – 181

Pyridoxal phosphate binding By similarity

Sites

Binding site

Allosteric inhibitor By similarity

Binding site

Pyridoxal phosphate By similarity

Binding site

268

Allosteric inhibitor; via amide nitrogen By similarity

Binding site

272

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

316

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P45040-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CA753FC79BBD05BD
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FASTA

316

33,384

        10         20         30         40         50         60 
MAIYADNSYS IGNTPLVRLK HFGHNGNVVV KIEGRNPSYS VKCRIGANMV WQAEKDGTLT 

        70         80         90        100        110        120 
KGKEIVDATS GNTGIALAYV AAARGYKITL TMPETMSLER KRLLCGLGVN LVLTEGAKGM 

       130        140        150        160        170        180 
KGAIAKAEEI VASDPSRYVM LKQFENPANP QIHRETTGPE IWKDTDGKVD VVVAGVGTGG 

       190        200        210        220        230        240 
SITGISRAIK LDFGKQITSV AVEPVESPVI SQTLAGEEVK PGPHKIQGIG AGFIPKNLDL 

       250        260        270        280        290        300 
SIIDRVETVD SDTALATARR LMAEEGILAG ISSGAAVAAA DRLAKLPEFA DKLIVVILPS 

       310 
ASERYLSTAL FEGIEG

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase." Huang B., Vetting M.W., Roderick S.L. J. Bacteriol. 187:3201-3205(2005) [PubMed: 15838047] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SAT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42023 Genomic DNA. Translation: AAC22758.1.

PIR

F64182.

RefSeq

NP_439260.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y7L	X-ray	1.55	A	1-316	[»]
3IQG	X-ray	1.90	X	1-316	[»]
3IQH	X-ray	1.90	X	1-316	[»]
3IQI	X-ray	1.70	X	1-316	[»]

ModBase

Search...

Genome annotation databases

GeneID

950077.

GenomeReviews

Gene locus HI1103 in contig L42023_GR.

KEGG

hin:HI1103.

NMPDR

fig|71421.1.peg.1060.

TIGR

HI1103.

Phylogenomic databases

HOGENOM

HBG748215.

OMA

SDPSRYV.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1103-MONOMER.

BRENDA

2.5.1.47. 109.

Family and domain databases

InterPro

IPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005859. CysK.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.

PROSITE

PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

CYSK_HAEIN

Accession

Primary (citable) accession number: P45040

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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