ID A0A1H3WYC7_9FIRM Unreviewed; 529 AA.
AC A0A1H3WYC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05216349_102267 {ECO:0000313|EMBL:SDZ92113.1};
OS Oribacterium sp. KHPX15.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=1855342 {ECO:0000313|EMBL:SDZ92113.1, ECO:0000313|Proteomes:UP000199483};
RN [1] {ECO:0000313|EMBL:SDZ92113.1, ECO:0000313|Proteomes:UP000199483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHPX15 {ECO:0000313|EMBL:SDZ92113.1,
RC ECO:0000313|Proteomes:UP000199483};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNRG01000002; SDZ92113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3WYC7; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000199483; 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; IPR023425; GalP_uridyl_Trfase_II_CS.
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.
DR PROSITE; PS01163; GAL_P_UDP_TRANSF_II; 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:UP000199483};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00571}.
FT DOMAIN 83..258
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 273..460
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
SQ SEQUENCE 529 AA; 60581 MW; AA897FBC05BD64E0 CRC64;
MDLQCGIKNL VAYAYRTTLI EEEDITWALN TVALNLKVDE VTSTKDEVME EAEKIPFDEV
EAEEFKTTTE TGIVDDGSYL ENVLKVLNDY AVEQGLTDGD SVVYRDLFDT KLMGALTPRP
SEVQANFFDL YEEDPKVATD WYYTFCRDTD YIRRYRVKKD LKWKTETEYG ELDITINLSK
PEKDPKAIAA AGKAKQTGYP KCQLCCECEG YAGRVDYPAR ENHRIIPIEI QGQEWGFQYS
PYVYYNEHCI VLNTKHTPMK IDKSAFLKLF DFVRQFPHYF VGSNADLPIV GGSILAHEHF
QGGNYEFAMA KAPVERSFTI PGYEDIKAGV VKWPMSVIRL TGENIAKMAD LADHILVAWR
GYTDEAAFIF AETDGVPHST ITPIARKVGE EYQLDLVLRN NITTEEHPLG VYHPHAKLHH
IKKENIGLIE VMGLAVLPSR LKQEMAELKE AFLTGKDLRD IPELEKHADW FDAFMEEYYR
RDIEVTAENF DEILQDEIGK VFMHVLEDAG VYKRTPEGQA AFDRFIKTL
//
