Reviewed, UniProtKB/Swiss-Prot O31631 (METB_BACSU)

Names and origin

Protein names

Recommended name:
    Cystathionine gamma-synthase
      Short name=CGS
    EC=2.5.1.48
Alternative name(s):
    O-acetylhomoserine (thiol)-lyase
    EC=2.5.1.49
    O-acetylhomoserine sulfhydrylase
      Short name=OAH sulfhydrylase

Gene names

Name:	metB
Synonyms:	metI, yjcI
Ordered Locus Names:	BSU11870

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transformation of O-succinylhomoserine into cystathionine, as well as O-acetylhomoserine and sulfide into homocysteine. Ref.2
Catalytic activity	O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate. Ref.2 O-acetyl-L-homoserine + methanethiol = L-methionine + acetate. Ref.2
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Induction	Repressed by methionine. Ref.2
Disruption phenotype	Cannot grow with sulfate, cysteine or cystathionine as sole sulfur source. Ref.2
Sequence similarities	Belongs to the trans-sulfuration enzymes family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	O-acetylhomoserine aminocarboxypropyltransferase activity Inferred from electronic annotation. Source: EC cystathionine gamma-synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 373	373	Cystathionine gamma-synthase		PRO_0000360654
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O31631-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: A7B849C730213602	FASTA	373	41,705
	10 20 30 40 50 60 MSQHVETKLA QIGNRSDEVT GTVSAPIYLS TAYRHRGIGE STGFDYVRTK NPTRQLVEDA 70 80 90 100 110 120 IANLENGARG LAFSSGMAAI QTIMALFKSG DELIVSSDLY GGTYRLFENE WKKYGLTFHY 130 140 150 160 170 180 DDFSDEDCLR SKITPNTKAV FVETPTNPLM QEADIEHIAR ITKEHGLLLI VDNTFYTPVL 190 200 210 220 230 240 QRPLELGADI VIHSATKYLG GHNDLLAGLV VVKDERLGEE MFQHQNAIGA VLPPFDSWLL 250 260 270 280 290 300 MRGMKTLSLR MRQHQANAQE LAAFLEEQEE ISDVLYPGKG GMLSFRLQKE EWVNPFLKAL 310 320 330 340 350 360 KTICFAESLG GVESFITYPA TQTHMDIPEE IRIANGVCNR LLRFSVGIEH AEDLKEDLKQ 370 ALCQVKEGAV SFE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination." Auger S., Yuen W.H., Danchin A., Martin-Verstraete I. Microbiology 148:507-518(2002) [PubMed: 11832514] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, INDUCTION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB13044.1.
PIR	A69847.
RefSeq	NP_389069.1.
3D structure databases
HSSP	HSSP built from PDB template 1GC0 based on UniProtKB P13254.
ModBase	Search...
Genome annotation databases
GeneID	939812.
GenomeReviews	Gene locus BSU11870 in contig AL009126_GR.
KEGG	bsu:BSU11870.
NMPDR	fig|224308.1.peg.1188.
Organism-specific databases
SubtiList	BG13162. metI. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O31631.
OMA	MQEADIE.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1188-MON.
Family and domain databases
InterPro	IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PANTHER	PTHR11808. Cys_Met_Meta_PP. 1 hit.
Pfam	PF01053. Cys_Met_Meta_PP. 1 hit. [Graphical view]
PIRSF	PIRSF001434. CGS. 1 hit.
PROSITE	PS00868. CYS_MET_METAB_PP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METB_BACSU

Accession

Primary (citable) accession number: O31631

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 44 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)