ID A0A367GFT9_9FIRM Unreviewed; 517 AA.
AC A0A367GFT9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE Short=Gal-1-P uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
DE EC=2.7.7.12 {ECO:0000256|HAMAP-Rule:MF_00571};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00571};
GN Name=galT {ECO:0000256|HAMAP-Rule:MF_00571};
GN ORFNames=C4885_06420 {ECO:0000313|EMBL:RCH52297.1};
OS Subdoligranulum sp. APC924/74.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=2086273 {ECO:0000313|EMBL:RCH52297.1, ECO:0000313|Proteomes:UP000253465};
RN [1] {ECO:0000313|EMBL:RCH52297.1, ECO:0000313|Proteomes:UP000253465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APC924/74 {ECO:0000313|EMBL:RCH52297.1,
RC ECO:0000313|Proteomes:UP000253465};
RA Fitzgerald B.C., Shkoporov A.N., Ross P.R., Hill C.;
RT "Complete genome sequencing of Faecalibacterium prausnitzii strains
RT isolated from the human gut.";
RL Submitted (FEB-2018) 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, ECO:0000256|HAMAP-
CC Rule:MF_00571};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|HAMAP-Rule:MF_00571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00571}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 2 family. {ECO:0000256|ARBA:ARBA00008706, ECO:0000256|HAMAP-
CC Rule:MF_00571}.
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:RCH52297.1}.
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DR EMBL; PSQF01000017; RCH52297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367GFT9; -.
DR OrthoDB; 2293at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000253465; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00571; GalP_UDP_trans; 1.
DR InterPro; IPR000766; GalP_uridyl_Trfase_II.
DR InterPro; IPR005850; GalP_Utransf_C.
DR InterPro; IPR005849; GalP_Utransf_N.
DR PANTHER; PTHR39191:SF1; DUF4922 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR39191; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF006005; GalT_BS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00571};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00571};
KW Galactose metabolism {ECO:0000256|ARBA:ARBA00023144, ECO:0000256|HAMAP-
KW Rule:MF_00571};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00571}; Reference proteome {ECO:0000313|Proteomes:UP000253465};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00571}.
FT DOMAIN 28..240
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 256..431
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
SQ SEQUENCE 517 AA; 57945 MW; C94C8436F673EEDA CRC64;
MTAEQRDAAL ALDVERLLRF GRKHKLIKEL DAIVARNTLL DLLGLAQPSE ENVPKEDFDT
PAALLDEMVE LAAAKGLFDG SVPQYRINFE TRMMGALMPR ESEVCRKFRK LYAKGGPKAA
TDWFYDLCVV SNYIRTAQIA KNIQWNTATP YGELEITINL TKPEKDPKVI AMERLQPAAS
YPKCMLCKEN IGYAGRINFP ARQTHRIVPM NLAGETFYLQ YSPYAYFHEH CIMLNDSHKP
MEMDRHTLAE IFDFVAQFPH YTCGSNADLP IVGGSILSHS HFQGGRYVFP MQKAHIAVPL
RNVRYTGVKA GIVNWPVSTV RLVGRSSQEV QNAADDILRT WRDYSDTSVD IIAHTGDTPH
NTVTPILHYD ENDGYILDLA LRNNRTTEQY PDGIFHPHKE YHNIKKENIG LIEVMGLAIL
PARLKDQSAA IADILTGSAP NTSREAGSPL AVHADWIDGL IKKYGTGLKR EKAEAVLRDE
IGIVFSHVLE NAGVFKQDAA GQAAFLKFME SVGYRKA
//
