ID A0A2B4S082_STYPI Unreviewed; 959 AA.
AC A0A2B4S082;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:PFX22449.1};
GN ORFNames=AWC38_SpisGene13018 {ECO:0000313|EMBL:PFX22449.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX22449.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU000506}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000256|ARBA:ARBA00010951,
CC ECO:0000256|RuleBase:RU000506}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX22449.1}.
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DR EMBL; LSMT01000239; PFX22449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4S082; -.
DR STRING; 50429.A0A2B4S082; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004335; F:galactokinase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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 CDD; cd10328; SLC5sbd_YidK; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR Gene3D; 3.30.428.10; HIT-like; 2.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019539; GalKase_N.
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; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00209; galT_1; 1.
DR NCBIfam; TIGR00813; sss; 1.
DR PANTHER; PTHR11943; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR11943:SF1; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF00474; SSF; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54197; HIT-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000506};
KW Galactose metabolism {ECO:0000256|RuleBase:RU000506};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000506};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000506};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 352..380
FT /note="Galactokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10509"
FT DOMAIN 439..503
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 629..795
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 802..957
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
SQ SEQUENCE 959 AA; 105540 MW; 356A9F6D37BC666E CRC64;
MVWEVCAAVA MVLTAVVLLP RYLKGGIATV PQFLEARYDK ATKSITSGLF LTGYVVVFLP
IVLYSGALAL NNLFDVPALL GVSKTIALWI TVWSIGIIGS IYAIFGGLKA VAVSDTINAI
GLLIGGLLIP VFGLLLIGDG HLLEGLTKLA DKLPEKFNII GGSTASVPFG TIFTGMMLVQ
LFYWGTNQAI VQRALGAKNL AEGQKGLVYA ACVKVLIPVI VVLPGIIAFY VFDGHLENPD
EAYTELVKKV LPLGLVGFFA AVLFGAILSS FNSALNSSVT LFGLDIYKSY IKKNAKDEQV
VKIGKLFGVG LAILSMCVAP LIAKVPGGLF GYLQEANGCY SIPILTIVVV GVNLIGEHTD
YNNGFVFPAA IDKGICLGIA PSKSEKSGVF AVDLKDHFEF DTATAQKTHP NKTWVNYILG
IVEELRKKDI TLPNFSVCFS GDIPLGAGLS SSAALENAFV FALNHQFSLG LSPFEMVKIS
QKAEHHFVGV QCGIMDQYVS MFGIKDAALL LDCDTLQSQT YPIDLEDFEW LLVNTNVKHS
LNASAYNQRR ASCERVANTL QKKSLRQASF ALLEAHQKNI DAGDYQKACF VLAENQRVQK
AKEAFQDKDV AQLGNLLYAS HQGLSEDYER FNILTGEWVL VSPHRTKRPW QGQVEKTAKE
VRLSYDPDCY LCKGNKRANG DVNPDYESTF VFTNDFAALQ NEGVTLEKQA NGLLVSSTEK
GICKVVCFSP DHSKTLADME VSNIAKVVKV WQEEYQKLGA IDFINYVQIF ENKGVVMGCS
NPHPHGQIWA QSSVPNEVLK KDKQQKQYHQ EKNTSLLQDY TLQELQLNER VVYENEGFVV
LVPYWAVWPY ETMIIPKKHH PSIESLSDEE ACFFADAIAK ITKAYDKVFD CLFPYSSGIH
QAPTGVAKND HWHFHMSFYP PLLRSASVKK FMVGYEMFGM PQRDITAEAA AKTLLALMD
//
