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Database: UniProt
Entry: A0A1M5UHZ9_9CLOT
LinkDB: A0A1M5UHZ9_9CLOT
Original site: A0A1M5UHZ9_9CLOT 
ID   A0A1M5UHZ9_9CLOT        Unreviewed;       500 AA.
AC   A0A1M5UHZ9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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=SAMN02745207_01749 {ECO:0000313|EMBL:SHH62635.1};
OS   Clostridium grantii DSM 8605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121316 {ECO:0000313|EMBL:SHH62635.1, ECO:0000313|Proteomes:UP000184447};
RN   [1] {ECO:0000313|EMBL:SHH62635.1, ECO:0000313|Proteomes:UP000184447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8605 {ECO:0000313|EMBL:SHH62635.1,
RC   ECO:0000313|Proteomes:UP000184447};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXM01000008; SHH62635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5UHZ9; -.
DR   STRING; 1121316.SAMN02745207_01749; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000184447; 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   NCBIfam; TIGR01239; galT_2; 1.
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:UP000184447};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00571}.
FT   DOMAIN          20..232
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          248..428
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
SQ   SEQUENCE   500 AA;  57499 MW;  5649F18A7C77EF66 CRC64;
     MNINFEIERL IQYALHTNLI TESDKIYSRN RVLSILNLDS SEEVTVDLNS EYNLSDILDN
     ILNWSFENNL LESNSPVYRD LLDAEIMNCF MPRPSEVINT FNVKYSSNPE SATDYFYNLS
     IASNYIRKDR IDKNIVWKAP TEYGELDITI NLSKPEKDPK AIAAAKNMKS TSYPLCLLCK
     ENEGYKGRVN HPSRGNHRII PIELTKTQWF IQYSPYVYYN EHCIVFKGAH EPMIINKSSF
     DRLLEFTELF PHYFVGSNAD LPIVGGSILS HDHFQGGHYT FAMETAPIER KVELKSFPTI
     EAGIVKWPMS VLRISSENRE LLSEAAGIIL NKWRAYSDES VDVLAFTNET PHNTITPIAR
     RRGNLYELDL VLRNNRTSDE HPLGIFHPHD EVHHIKKENI GLIEVMGLAV LPARLETELS
     DLSAYLIDKE LILEDEELLK HASWLSLLRE KYTVSSEKEA MDVLKKEVGK KFMTVLEHAG
     VYKRDEKGEN AFVKFVESIK
//
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