[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=6361020 [NCBI, ExPASy, EBI, Israel, Japan] Duchange N., Zakin M.M., Ferrara P., Saint-Girons I., Park I., Tran S.V., Py M.-C., Cohen G.N.; "Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and of the 5'- and 3'-flanking regions of the metBL operon."; J. Biol. Chem. 258:14868-14871(1983).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan] Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."; Nucleic Acids Res. 21:3391-3398(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	PROTEIN SEQUENCE OF 182-209. DOI=10.1016/0006-291X(87)90968-5; PubMed=3307782 [NCBI, ExPASy, EBI, Israel, Japan] Martel A., Bouthier de la Tour C., Le Goffic F.; "Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences."; Biochem. Biophys. Res. Commun. 147:565-571(1987).
[6]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). DOI=10.1093/emboj/17.23.6827; PubMed=9843488 [NCBI, ExPASy, EBI, Israel, Japan] Clausen T., Huber R., Prade L., Wahl M.C., Messerschmidt A.; "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5-A resolution."; EMBO J. 17:6827-6838(1998).

Comments

CATALYTIC ACTIVITY: O⁴-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.
COFACTOR: Pyridoxal phosphate.
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway .
SUBUNIT: Homotetramer.
INTERACTION:
P18843:nadE; NbExp=1; IntAct=EBI-1134244, EBI-548960;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the trans-sulfuration enzymes family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K01546; AAA24167.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03071.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76921.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77371.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A01158; SYECCG.

RefSeq

AP_003870.1; -.
NP_418374.1; -.

3D structure databases

PDB

1CS1; X-ray; 1.50 A; A/B/C/D=1-386.

[ExPASy / RCSB / EBI]

PDBsum

1CS1; -.

ModBase

P00935.

Protein-protein interaction databases

DIP

DIP:10192N; -.

IntAct

P00935; -.

Enzyme and pathway databases

BioCyc

EcoCyc:O-SUCCHOMOSERLYASE-MON; -.
MetaCyc:O-SUCCHOMOSERLYASE-MON; -.

2D gel databases

ECO2DBASE

G040.1; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0577; -.

EcoGene

EG10582; metB.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
IPR011821; O_succ_thio_ly.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR015422; PyrdxlP-dep_Trfase_major_sub2.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.

PANTHER

PTHR11808; Cys_Met_Meta_PP; 1.

Pfam

PF01053; Cys_Met_Meta_PP; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001434; CGS; 1.

TIGRFAMs

TIGR02080; O_succ_thio_ly; 1.

PROSITE

PS00868; CYS_MET_METAB_PP; 1.

BLOCKS

P00935.

Genome annotation databases

GeneID

948434; -.

GenomeReviews

U00096_GR; b3939.
AP009048_GR; JW3910.

KEGG

ecj:JW3910; -.
eco:b3939; -.

Phylogenomic databases

HOGENOM

P00935; -.

Genome annotation databases

CMR

P00935; b3939.

Other

ProtoNet

P00935.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; Methionine biosynthesis; Pyridoxal phosphate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 386`	`386`	`Cystathionine gamma-synthase.`	`PRO_0000114756`
`BINDING`	`198 198`		`Pyridoxal phosphate (covalent).`
`HELIX`	`5 11`	`7`
`TURN`	`12 15`	`4`
`TURN`	`18 20`	`3`
`STRAND`	`22 24`	`3`
`STRAND`	`31 33`	`3`
`TURN`	`47 49`	`3`
`HELIX`	`52 65`	`14`
`STRAND`	`68 75`	`8`
`HELIX`	`76 87`	`12`
`STRAND`	`93 97`	`5`
`HELIX`	`102 112`	`11`
`TURN`	`113 115`	`3`
`STRAND`	`118 122`	`5`
`HELIX`	`127 135`	`9`
`STRAND`	`139 144`	`6`
`TURN`	`148 150`	`3`
`HELIX`	`156 165`	`10`
`STRAND`	`169 173`	`5`
`TURN`	`175 177`	`3`
`TURN`	`179 181`	`3`
`HELIX`	`184 187`	`4`
`STRAND`	`190 195`	`6`
`TURN`	`196 201`	`6`
`STRAND`	`209 215`	`7`
`HELIX`	`216 228`	`13`
`HELIX`	`235 245`	`11`
`HELIX`	`248 266`	`19`
`STRAND`	`272 276`	`5`
`HELIX`	`286 292`	`7`
`STRAND`	`298 306`	`9`
`HELIX`	`308 316`	`9`
`STRAND`	`319 325`	`7`
`STRAND`	`329 331`	`3`
`STRAND`	`333 336`	`4`
`HELIX`	`337 339`	`3`
`TURN`	`340 344`	`5`
`HELIX`	`347 352`	`6`
`STRAND`	`359 363`	`5`
`HELIX`	`369 383`	`15`

Sequence information

Length: 386 AA [This is the length of the unprocessed precursor]

Molecular weight: 41550 Da [This is the MW of the unprocessed precursor]

CRC64: 423B825219A42E9E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG NPTRDVVQRA 

        70         80         90        100        110        120 
LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGCYRVL 

       130        140        150        160        170        180 
FVDQGDEQAL RAALAEKPKL VLVESPSNPL LRVVDIAKIC HLAREVGAVS VVDNTFLSPA 

       190        200        210        220        230        240 
LQNPLALGAD LVLHSCTKYL NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL 

       250        260        270        280        290        300 
LLRGLRTLVP RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML 

       310        320        330        340        350        360 
SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR AAAGISETLL 

       370        380 
RISTGIEDGE DLIADLENGF RAANKG

P00935 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools