GAL7_THEMA
ID GAL7_THEMA Reviewed; 318 AA.
AC O33836;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12 {ECO:0000250|UniProtKB:P09148};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=galT; OrderedLocusNames=TM_1191;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9741105; DOI=10.1016/s0723-2020(98)80002-7;
RA Liebl W., Wagner B., Schellhase J.;
RT "Properties of an alpha-galactosidase, and structure of its gene galA,
RT within an alpha- and beta-galactoside utilization gene cluster of the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL Syst. Appl. Microbiol. 21:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-
CC glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989,
CC ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:66914; EC=2.7.7.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09148};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P09148};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
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DR EMBL; AJ001072; CAA04515.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36266.1; -; Genomic_DNA.
DR PIR; D72283; D72283.
DR RefSeq; NP_228996.1; NC_000853.1.
DR RefSeq; WP_004080138.1; NZ_CP011107.1.
DR AlphaFoldDB; O33836; -.
DR SMR; O33836; -.
DR STRING; 243274.THEMA_08375; -.
DR PRIDE; O33836; -.
DR EnsemblBacteria; AAD36266; AAD36266; TM_1191.
DR KEGG; tma:TM1191; -.
DR eggNOG; COG1085; Bacteria.
DR InParanoid; O33836; -.
DR OMA; QIWANEQ; -.
DR OrthoDB; 1064872at2; -.
DR BioCyc; MetaCyc:MON-506; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
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;
KW Carbohydrate metabolism; Galactose metabolism; Iron; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..318
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169898"
FT ACT_SITE 143
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 130
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 145
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P09148"
SQ SEQUENCE 318 AA; 37633 MW; E913778A6D770C6E CRC64;
MMELRYNPLT DEWVIVSAAT QKRPVQPSKT ECPICVGGLE LPEEYDLVTF ENRYPSLKKD
PPPVNWKEKG PFRKEESRGV CEVVVYTSDH NTALPGMPLK QIEKLVEMWV DRTRDLSQHD
FVKYIFIFEN RGKEVGASLP HPHGQIYAFP FLPKRIEVKI GAMRKWYEEK RKCPICEVLE
SEGEERKVYE TEHFLALVPF YARFPYEVHI YPKRHVSTLL EFSKEEKKEF AKVLKVVTAK
YDKLFDQEFP YMMMFFQAPF NEEDVSHFFH FHVEFNPPKR DRDKLKWMAS VETGTWAFIN
PVVPEEAARQ LRETEVEI
