NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2198256 [NCBI, ExPASy, EBI, Israel, Japan]
Houng H.S.H., Kopecko D.J., Baron L.S.;
"Molecular cloning and physical and functional characterization of the Salmonella typhimurium and Salmonella typhi galactose utilization operons.";
J. Bacteriol. 172:4392-4398(1990).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).

Comments

CATALYTIC ACTIVITY: ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate.
PATHWAY: Carbohydrate metabolism; galactose metabolism .
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.

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

M33681; AAA27113.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008731; AAL19712.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C37760; C37760.

RefSeq

NP_459753.1; -.

3D structure databases

ModBase

P22713.

Enzyme and pathway databases

BioCyc

STYP99287:STM0774-MON; -.

Organism-specific databases

StyGene

SG10137; galK.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004335;	Molecular function: galactokinase activity (inferred from electronic annotation from HAMAP).
GO:0046835;	Biological process: carbohydrate phosphorylation (inferred from electronic annotation from InterPro).
GO:0006012;	Biological process: galactose metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00246; -; 1.
PBIL [Tree]

InterPro

IPR000705; Galactokinase.
IPR006204; GHMP_kinase.
IPR013750; GHMP_kinase_C.
IPR006203; GHMP_knse_ATP_bd_CS.
IPR006206; Mev_galkinase.
IPR014721; Ribosomal_S5_D2-type_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.

Pfam

PF08544; GHMP_kinases_C; 1.
PF00288; GHMP_kinases_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000530; Galactokinase; 1.

PRINTS

PR00473; GALCTOKINASE.
PR00959; MEVGALKINASE.

TIGRFAMs

TIGR00131; gal_kin; 1.

PROSITE

PS00106; GALACTOKINASE; 1.
PS00627; GHMP_KINASES_ATP; 1.

ProtoNet

P22713.

Genome annotation databases

GeneID

1252294; -.

GenomeReviews

AE006468_GR; STM0774.

KEGG

stm:STM0774; -.

NMPDR

fig|99287.1.peg.741; -.

Phylogenomic databases

HOGENOM

P22713; -.

Genome annotation databases

CMR

P22713; STM0774.

Other

UniRef

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

Keywords

ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm; Galactose metabolism; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`Galactokinase.`	`PRO_0000184622`
`NP_BIND`	`122 132`	`11`	`ATP (Potential).`
`CONFLICT`	`6 9`		`KTRA -> NASR (in Ref. 1; AAA27113).`
`CONFLICT`	`105 105`		`Q -> L (in Ref. 1; AAA27113).`
`CONFLICT`	`119 119`		`Missing (in Ref. 1; AAA27113).`
`CONFLICT`	`151 151`		`Missing (in Ref. 1; AAA27113).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41302 Da [This is the MW of the unprocessed precursor]

CRC64: 754143671EAF2E8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLKEKTRAL FAEIFGYPAT HTIQAPGRVN LIGEHTDYND GFVLPCAIDY QTVISCAPRD 

        70         80         90        100        110        120 
DRTVRVIAAD YDNQVDEFSL DAPIVTHDSQ QWSNYVRGVV KHLQQRNNAF GGVDMVISGN 

       130        140        150        160        170        180 
VPQGAGLSSS ASLEVAVGTV FQQLYHLPLD GAQIALNGQE AENQFVGCNC GIMDQLISAL 

       190        200        210        220        230        240 
GKKDHALLID CRTLGAKAVS MPKGVAVVII NSNFKRTLVG SEYNTRREQC ETGARFFQQP 

       250        260        270        280        290        300 
ALRDVSLEAF NAVASELDPV VAKRVRHVLS ENARTVEAAS ALEKGDLQRM GQLMAESHAS 

       310        320        330        340        350        360 
MRDDFEITVP QIDTLVDIVK ATIGDRGGVR MTGGGFGGCV VALIPEDLVP AVRQAVAQQY 

       370        380 
EAKTGIKETF YVCKPSQGAG QC

P22713 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