(data stored in SCRATCH zone)

SWISSPROT: D6XXA3_BACIE

ID   D6XXA3_BACIE            Unreviewed;       504 AA.
AC   D6XXA3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE            Short=Gal-1-P uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE            EC=2.7.7.12 {ECO:0000256|HAMAP-Rule:MF_00571};
DE   AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
GN   Name=galT {ECO:0000256|HAMAP-Rule:MF_00571};
GN   OrderedLocusNames=Bsel_0421 {ECO:0000313|EMBL:ADH97960.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97960.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97960.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose =
CC         alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose;
CC         Xref=Rhea:RHEA:13989, ChEBI:CHEBI:58336, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=2.7.7.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00571};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00571}.
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate
CC       uridylyltransferase type 2 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00571}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001791; ADH97960.1; -; Genomic_DNA.
DR   RefSeq; WP_013171389.1; NC_014219.1.
DR   STRING; 439292.Bsel_0421; -.
DR   EnsemblBacteria; ADH97960; ADH97960; Bsel_0421.
DR   KEGG; bse:Bsel_0421; -.
DR   eggNOG; ENOG4105CKN; Bacteria.
DR   eggNOG; COG4468; LUCA.
DR   HOGENOM; HOG000244460; -.
DR   KO; K00965; -.
DR   OMA; IVDWPMS; -.
DR   OrthoDB; 801432at2; -.
DR   BioCyc; BSEL439292:G1GLR-451-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00571; GalP_UDP_trans; 1.
DR   InterPro; IPR000766; GalP_uridyl_Trfase_II.
DR   InterPro; IPR023425; GalP_uridyl_Trfase_II_CS.
DR   InterPro; IPR005850; GalP_Utransf_C.
DR   InterPro; IPR005849; GalP_Utransf_N.
DR   PANTHER; PTHR39191; PTHR39191; 1.
DR   Pfam; PF02744; GalP_UDP_tr_C; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF006005; GalT_BS; 1.
DR   TIGRFAMs; TIGR01239; galT_2; 1.
DR   PROSITE; PS01163; GAL_P_UDP_TRANSF_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XXA3.
DR   SWISS-2DPAGE; D6XXA3.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00571};
KW   Galactose metabolism {ECO:0000256|HAMAP-Rule:MF_00571};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00571,
KW   ECO:0000313|EMBL:ADH97960.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00571,
KW   ECO:0000313|EMBL:ADH97960.1}.
FT   DOMAIN       18    232       GalP_UDP_transf. {ECO:0000259|Pfam:
FT                                PF01087}.
FT   DOMAIN      247    446       GalP_UDP_tr_C. {ECO:0000259|Pfam:
FT                                PF02744}.
SQ   SEQUENCE   504 AA;  57609 MW;  5CC802B7C636A5CA CRC64;
     MEQTLNELIS YALERELIEE ADTVYVKNRL LDAMGLTEGE TDAFQRSEEI RPLYTILDEL
     TDDALKRGLI EDDTVTMRDL FDTELMGILT DRPAHVIRTF RDIEREQGIE AATAWFYEFS
     QDVHYIRRER IAKNRSWQTE TDYGALDITI NLSKPEKDPK EIAKAKEAGE ANYPLCLLCK
     ENEGYSGRVN HPARQNLRVI PVTLAGDPWF VQFSPYVYYH EHAIVLSSAH EPMSIRRKTF
     ERLLDFVEQY PHYFIGSNAD LPIVGGSILS HDHYQAGKYE FPMARAEMEE ERSLERFADV
     TVGRVKWPMS VVRVKGESKA AVIMASEHIL QGWRHYTDES VDVRAFTGDT PHHTITPIAR
     KRDGQFELDL VLRDNQTSSE HPSGIYHPHE DVHHIKKENI GLIEVMGLAV LPGRLDSELK
     ALQEALAAED PSGAIQSDEA IQKHHDWAMA ILSRYGDVAG DQGTRILQEE VGQVFHEILH
     HSGVFKRDDE GQAAFTRFLE TLTR
//

If you have problems or comments...

PBIL Back to PBIL home page