(data stored in ACNUC7421 zone)

SWISSPROT: B7ULN1_ECO27

ID   B7ULN1_ECO27            Unreviewed;       348 AA.
AC   B7ULN1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 60.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|RuleBase:RU000506};
DE            EC=2.7.7.12 {ECO:0000256|RuleBase:RU000506};
GN   Name=galT {ECO:0000313|EMBL:CAS08183.1};
GN   OrderedLocusNames=E2348C_0635 {ECO:0000313|EMBL:CAS08183.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08183.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08183.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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|PROSITE-ProRule:PRU10033,
CC         ECO:0000256|RuleBase:RU000506};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000808-4};
CC       Note=Binds 1 Fe cation per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000808-4};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000808-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000808-
CC       3};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|RuleBase:RU000506}.
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate
CC       uridylyltransferase type 1 family.
CC       {ECO:0000256|RuleBase:RU000506}.
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DR   EMBL; FM180568; CAS08183.1; -; Genomic_DNA.
DR   RefSeq; WP_000191523.1; NC_011601.1.
DR   EnsemblBacteria; CAS08183; CAS08183; E2348C_0635.
DR   KEGG; ecg:E2348C_0635; -.
DR   HOGENOM; HOG000230490; -.
DR   KO; K00965; -.
DR   OMA; HAIYYPP; -.
DR   BioCyc; ECOL574521:E2348C_RS03410-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:InterPro.
DR   CDD; cd00608; GalT; 1.
DR   Gene3D; 3.30.428.10; -; 2.
DR   InterPro; IPR001937; GalP_UDPtransf1.
DR   InterPro; IPR019779; GalP_UDPtransf1_His-AS.
DR   InterPro; IPR005850; GalP_Utransf_C.
DR   InterPro; IPR005849; GalP_Utransf_N.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR11943; PTHR11943; 1.
DR   Pfam; PF02744; GalP_UDP_tr_C; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF000808; GalT; 1.
DR   SUPFAM; SSF54197; SSF54197; 2.
DR   TIGRFAMs; TIGR00209; galT_1; 1.
DR   PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7ULN1.
DR   SWISS-2DPAGE; B7ULN1.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000506};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Galactose metabolism {ECO:0000256|RuleBase:RU000506};
KW   Iron {ECO:0000256|PIRSR:PIRSR000808-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000808-3,
KW   ECO:0000256|RuleBase:RU000506};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000506,
KW   ECO:0000313|EMBL:CAS08183.1};
KW   Transferase {ECO:0000256|RuleBase:RU000506,
KW   ECO:0000313|EMBL:CAS08183.1}; Zinc {ECO:0000256|PIRSR:PIRSR000808-3}.
FT   DOMAIN        3    176       GalP_UDP_transf. {ECO:0000259|Pfam:
FT                                PF01087}.
FT   DOMAIN      183    345       GalP_UDP_tr_C. {ECO:0000259|Pfam:
FT                                PF02744}.
FT   REGION       28     31       UDP-alpha-D-glucose binding; shared with
FT                                dimeric partner. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
FT   REGION       77     78       UDP-alpha-D-glucose binding.
FT                                {ECO:0000256|PIRSR:PIRSR000808-2}.
FT   REGION      159    161       UDP-alpha-D-glucose binding.
FT                                {ECO:0000256|PIRSR:PIRSR000808-2}.
FT   REGION      311    312       UDP-alpha-D-glucose binding; shared with
FT                                dimeric partner. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
FT   REGION      316    317       UDP-alpha-D-glucose binding; shared with
FT                                dimeric partner. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
FT   ACT_SITE    166    166       Tele-UMP-histidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000808-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10033}.
FT   METAL        52     52       Zinc. {ECO:0000256|PIRSR:PIRSR000808-3}.
FT   METAL        55     55       Zinc. {ECO:0000256|PIRSR:PIRSR000808-3}.
FT   METAL       115    115       Zinc. {ECO:0000256|PIRSR:PIRSR000808-3}.
FT   METAL       164    164       Zinc. {ECO:0000256|PIRSR:PIRSR000808-3,
FT                                ECO:0000256|PROSITE-ProRule:PRU10033}.
FT   METAL       182    182       Iron. {ECO:0000256|PIRSR:PIRSR000808-4}.
FT   METAL       281    281       Iron. {ECO:0000256|PIRSR:PIRSR000808-4}.
FT   METAL       296    296       Iron. {ECO:0000256|PIRSR:PIRSR000808-4}.
FT   METAL       298    298       Iron. {ECO:0000256|PIRSR:PIRSR000808-4}.
FT   BINDING      61     61       UDP-alpha-D-glucose; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000808-2}.
FT   BINDING     153    153       UDP-alpha-D-glucose. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
FT   BINDING     168    168       UDP-alpha-D-glucose. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
FT   BINDING     323    323       UDP-alpha-D-glucose. {ECO:0000256|PIRSR:
FT                                PIRSR000808-2}.
SQ   SEQUENCE   348 AA;  39622 MW;  713DA64DC07A4D63 CRC64;
     MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP DCFLCAGNVR
     VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESNDPLMRCQ SARGTSRVIC FSPDHSKTLP
     ELSVAALTKI VKTWQEQTAE LGKTYPWVQV FENKGAAMGC SNPHPHGQIW ANSFLPNEAE
     REDRLQKEYF AEQKSPMLVD YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH
     VLRITDLTDA QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY
     PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV
//

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