ID   GAL7_STRLI              Reviewed;         354 AA.
AC   P13212;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 111.
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;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3335481; DOI=10.1128/jb.170.1.203-212.1988;
RA   Adams C.W., Fornwald J.A., Schmidt F.J., Rosenberg M., Brawner M.E.;
RT   "Gene organization and structure of the Streptomyces lividans gal operon.";
RL   J. Bacteriol. 170:203-212(1988).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RA   Gibson T.J.;
RL   Unpublished observations (MAR-1995).
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         Evidence={ECO:0000250|UniProtKB:P09148};
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26746.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M18953; AAA26746.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A28669; XNSMUD.
DR   AlphaFoldDB; P13212; -.
DR   SMR; P13212; -.
DR   UniPathway; UPA00214; -.
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   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; Transferase; Zinc.
FT   CHAIN           1..354
FT                   /note="Galactose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000169897"
FT   REGION          36..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        167
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P09148"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P09148"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT   BINDING         154
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P09148"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT   BINDING         169
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P09148"
FT   BINDING         332
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P09148"
FT   CONFLICT        59..75
FT                   /note="QGRTYHPPADQCPLCPS -> AGAHLPSAGRPVPAVPV (in Ref. 1;
FT                   AAA26746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307..354
FT                   /note="NFSLPPYVRQAEVPRGLRIRHERVHQRDVPPERAAERLREVADVHERE ->
FT                   ELFTSAVRPAS (in Ref. 1; AAA26746)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  40095 MW;  73B3BA8C2DAC9BA2 CRC64;
     MKKTSTRLAD GRELVYYDLR DDTVRDAVDR RPLERTVTTS EVRRDPLLGD SAPSRLAPQG
     RTYHPPADQC PLCPSGRGTA ERDPAYDVVV FENRFPSLAG DSGRCEVVCF TSDHDASFAD
     LSEEQARLVV DAWTDRTSEL SHLPSVEQVF CFENRGAEIG VTLGHPHGQI YAYPFTTPRT
     ALMLRSLAAH KDATGGGNLF DSVLEEELAG ERVVLEGEHW AAFVAYGAHW PYEVHLYPKR
     RVPDLLGLDE AARTEFPKVY LELLRRFDRI FGEGEPPTPY IAAWHQAPFG QLEFEGVTRD
     DFALHLNFSL PPYVRQAEVP RGLRIRHERV HQRDVPPERA AERLREVADV HERE