GAL7_HAEIN
ID GAL7_HAEIN Reviewed; 349 AA.
AC P31764;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=HI_0820;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RM 7004 / Serotype B;
RX PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x;
RA Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.;
RT "The gal locus from Haemophilus influenzae: cloning, sequencing and the use
RT of gal mutants to study lipopolysaccharide.";
RL Mol. Microbiol. 6:3051-3063(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(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. Zinc binding seems to play a
CC structural role. {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; X65934; CAA46730.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22479.1; -; Genomic_DNA.
DR PIR; E64096; E64096.
DR RefSeq; NP_438980.1; NC_000907.1.
DR RefSeq; WP_005693184.1; NC_000907.1.
DR AlphaFoldDB; P31764; -.
DR SMR; P31764; -.
DR STRING; 71421.HI_0820; -.
DR EnsemblBacteria; AAC22479; AAC22479; HI_0820.
DR KEGG; hin:HI_0820; -.
DR PATRIC; fig|71421.8.peg.861; -.
DR eggNOG; COG1085; Bacteria.
DR HOGENOM; CLU_029960_0_0_6; -.
DR OMA; HAIYYPP; -.
DR PhylomeDB; P31764; -.
DR BioCyc; HINF71421:G1GJ1-861-MON; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000579; 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..349
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169895"
FT ACT_SITE 167
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 29..32
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 78..79
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 116
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 /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 160..162
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
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 /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 312..313
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 317..318
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 324
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT VARIANT 221
FT /note="I -> V (in strain: RM 7004)"
FT VARIANT 229
FT /note="I -> V (in strain: RM 7004)"
FT VARIANT 334
FT /note="E -> D (in strain: RM 7004)"
SQ SEQUENCE 349 AA; 40758 MW; 3BAB24B417E5ECBF CRC64;
MTALFEPTEH PHRRYNPLID QWVLVSPHRA KRPWQGQQEK VNEEQKPSYD PTCYLCPSNK
RITGELNPDY RKPYVFKNDF SALLEDTPAP EKSSDPLFQS SQARGESRVI CFSPDHSKTL
PLLTALEIEE VIKVWQEQLR ELGAKYQWVQ IFENKGAAMG CSNPHPHGQI WANSFLPNEV
AREDRTQRDY LLKHGSVMLV DYVKRELALK ERIVVETEHW IALVPYWAIW PFETLLLPKT
HVKRLTELSD EQSKDLAVIL KKLTTKYDNL FETSFPYSMG FHAAPFNGED NEHWQLHAHF
YPPLLRSATV RKFMVGYEML GENQRDLTAE QAAERLRALS EVHYKERTK
