P45875 (GST_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase GST-4.5
EC=2.5.1.18

Gene names

Name:	gst
Ordered Locus Names:	XCC0929

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the GST superfamily. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase 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 – 204	204	Glutathione S-transferase GST-4.5		PRO_0000185976
Regions
	Domain	1 – 77	77	GST N-terminal
	Domain	83 – 204	122	GST C-terminal
	Region	61 – 62	2	Glutathione binding By similarity
Sites
	Binding site	10	1	Glutathione By similarity
	Binding site	49	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	102	1	Glutathione By similarity
Experimental info
	Sequence conflict	22	1	C → G AA sequence Ref.2
	Sequence conflict	26	1	E → D AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P45875 [UniParc]. Last modified July 11, 2002. Version 3. Checksum: F6302C321EB1F86F	FASTA	204	22,321
	10 20 30 40 50 60 MKLYTKPGAC SLADHIVLRW SCLPFELTVV DAATMKSPDY LRLNPAGAVP LLVVDQWALT 70 80 90 100 110 120 QNAAILNYIA DTAPLTGLGG DGTARSRAEI NRWIAFVNAD LHPTFKPLFG STAYLQEDAL 130 140 150 160 170 180 IQRSHEDART KLRTLYTRVD AHLQGRNWLA GDTHTGADAY LFVTLRWAHK AGVDLSGLSA 190 200 LDAFFQRMLA DADVQAALQA EGLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.
[2]	"Characterization of glutathione transferase from Xanthomonas campestris." di Ilio C., Aceto A., Allocati N., Piccolomini R., Bucciarelli T., Dragani B., Faraone A., Sacchetta P., Petruzzelli R., Federici G. Arch. Biochem. Biophys. 305:110-114(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40239.1.
PIR	S35583.
RefSeq	NP_636315.1. NC_003902.1.
3D structure databases
ProteinModelPortal	P45875.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC0929.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM40239; AAM40239; XCC0929.
GeneID	1001477.
KEGG	xcc:XCC0929.
PATRIC	24072543. VBIXanCam115730_1001.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000125748.
KO	K00799.
OMA	AHIVLEW.
ProtClustDB	CLSK881285.
Enzyme and pathway databases
BioCyc	XCAM190485:GIXZ-928-MONOMER.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GST_XANCP

Accession

Primary (citable) accession number: P45875

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 11, 2002
Last modified:	May 29, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program