ID A0A1X7FTS0_9ACTN Unreviewed; 351 AA.
AC A0A1X7FTS0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00016340, ECO:0000256|RuleBase:RU000506};
DE EC=2.7.7.12 {ECO:0000256|ARBA:ARBA00012384, ECO:0000256|RuleBase:RU000506};
GN ORFNames=SAMN02745830_04614 {ECO:0000313|EMBL:SMF58616.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF58616.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF58616.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF58616.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001107,
CC ECO:0000256|RuleBase:RU000506};
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:PIRSR000808-3};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU000506}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000256|ARBA:ARBA00010951,
CC ECO:0000256|RuleBase:RU000506}.
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; FWZW01000010; SMF58616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FTS0; -.
DR OrthoDB; 9769064at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000192930; Unassembled WGS sequence.
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; HIT-like; 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 NCBIfam; TIGR00209; galT_1; 1.
DR PANTHER; PTHR11943; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR11943:SF1; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF000808; GalT; 1.
DR SUPFAM; SSF54197; HIT-like; 2.
DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000506};
KW Galactose metabolism {ECO:0000256|RuleBase:RU000506};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000808-3};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000506};
KW Reference proteome {ECO:0000313|Proteomes:UP000192930};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT DOMAIN 102..177
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 198..350
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
FT ACT_SITE 169
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
SQ SEQUENCE 351 AA; 39674 MW; 97866830675EA168 CRC64;
MKKTSTRLAD GRELIYYDQR DDSVRDAVDR RPLDRTVTTS EVRRDPLLGD AVAIASHRQG
RTYHPPADEC PLCPSQGDRL SEIPDSSYDV VVFENRFPSL AGDSGRCEVV CFTSDHDASF
ADLTEAQARL VLDAWTDRTS ELSHLPSVEQ VFCFENRGAE IGVTLGHPHG QIYAYPFTTP
RTALMLRSLA AHREATGGEN LFDAVLEREL AGERVVLESE HWAAFVPYAA HWPYEVHLYP
KRRVPDLLAL DEAARTEFPQ VYLELLRRFD RIFGEGEPPT PYIAAWHQAP FRLEEFEGVN
RDDFALHLEL FTVRRTSGKL KFLAGSESGM SVFINDVPPE RAAERLREVA S
//
