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: UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Carbohydrate metabolism; galactose metabolism .
SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 1 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

M33681; AAA27112.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008731; AAL19713.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B37760; B37760.

RefSeq

NP_459754.1; -.

3D structure databases

HSSP

P09148; 1HXP. [HSSP ENTRY / PDB]

SMR

P22714; 2-348.

ModBase

P22714.

Enzyme and pathway databases

BioCyc

STYP99287:STM0775-MON; -.

Organism-specific databases

StyGene

SG10138; galT.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008108;	Molecular function: UDP-glucose:hexose-1-phosphate uridylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006012;	Biological process: galactose metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001937; GalP_UDPtransf1.
IPR005850; GalP_Utransf_C.
IPR005849; GalP_Utransf_N.
IPR011151; His_triad_motif.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.428.10; His_triad_motif; 2.

PANTHER

PTHR11943; GalP_UDPtransf1; 1.

Pfam

PF02744; GalP_UDP_tr_C; 1.
PF01087; GalP_UDP_transf; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000808; GalT; 1.

ProDom

PD005051; GalP_Utransf; 2.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00209; galT_1; 1.

PROSITE

PS00117; GAL_P_UDP_TRANSF_I; 1.

ProtoNet

P22714.

Genome annotation databases

GeneID

1252295; -.

GenomeReviews

AE006468_GR; STM0775.

KEGG

stm:STM0775; -.

Phylogenomic databases

HOGENOM

P22714; -.

Genome annotation databases

CMR

P22714; STM0775.

Other

UniRef

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

Keywords

Carbohydrate metabolism; Complete proteome; Galactose metabolism; Iron; Metal-binding; Nucleotidyltransferase; Transferase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Galactose-1-phosphate uridylyltransferase.`	`PRO_0000169896`
`ACT_SITE`	`166 166`		`Tele-UMP-histidine intermediate (By similarity).`
`METAL`	`52 52`		`Zinc (By similarity).`
`METAL`	`55 55`		`Zinc (By similarity).`
`METAL`	`115 115`		`Zinc (By similarity).`
`METAL`	`164 164`		`Zinc (By similarity).`
`METAL`	`182 182`		`Iron (By similarity).`
`METAL`	`281 281`		`Iron (By similarity).`
`METAL`	`296 296`		`Iron (By similarity).`
`METAL`	`298 298`		`Iron (By similarity).`
`CONFLICT`	`31 31`		`Missing (in Ref. 1; AAA27112).`
`CONFLICT`	`180 180`		`E -> AE (in Ref. 1).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 39675 Da [This is the MW of the unprocessed precursor]

CRC64: 2D2CA786668A178E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTPFNPIDHP HRRYNPLTGQ WVLVSPHRAK RPWQGAQETP SQQMLPAHDP DCFLCAGNTR 

        70         80         90        100        110        120 
VTGDKNPDYK GTYVFTNDFA ALMADTPDAP DSHDPLMRCQ SARGTSRVIC FSPDHSKTLP 

       130        140        150        160        170        180 
ELSLPALTEI VRTWQTQTAE LGKTYPWVQV FENKGAAMGC SNPHPHGQVW ANSFLPNEAE 

       190        200        210        220        230        240 
REDRLQKAYF AEQRSPMLVD YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKTH 

       250        260        270        280        290        300 
VLRITDLSDE QRDSLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN AHWQLHAHFY 

       310        320        330        340 
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV

P22714 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