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Database: UniProt
Entry: R5PV16_9FIRM
LinkDB: R5PV16_9FIRM
Original site: R5PV16_9FIRM 
ID   R5PV16_9FIRM            Unreviewed;       499 AA.
AC   R5PV16;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=BN766_01358 {ECO:0000313|EMBL:CCZ20395.1};
OS   Candidatus Apopatosoma intestinale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Apopatosoma.
OX   NCBI_TaxID=1262966 {ECO:0000313|EMBL:CCZ20395.1, ECO:0000313|Proteomes:UP000018243};
RN   [1] {ECO:0000313|EMBL:CCZ20395.1, ECO:0000313|Proteomes:UP000018243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:724 {ECO:0000313|Proteomes:UP000018243};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ20395.1}.
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DR   EMBL; CAZP010000098; CCZ20395.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PV16; -.
DR   STRING; 1262966.BN766_01358; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000018243; 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:UP000018243};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00571}.
FT   DOMAIN          19..230
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          246..431
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
SQ   SEQUENCE   499 AA;  56424 MW;  2F29ACE16FAAEB52 CRC64;
     MISERIKQLV NYGAEKKLIT EADRIYATNL LLDAMGEQSY EDPGEVPAAS LEEILGALCD
     IAEEKGIIAE KGSVVRRDLF DTRLMGLLTP RPSEVIAKFR SEYEKSPEAA TDFYYNFSKN
     TDYIRTYRVK KDIRWTVPSE FGEIDITINL SKPEKDPKDI ALAKMQQQSS YPKCALCPEN
     EGYAGNMSAA ARENHRLIPI TLGGEKWFFQ YSPYVYYNEH CIALSAEHTP MNVCVKTVER
     MLDFIDIFPH YFIGSNAGLP IVGGSILTHD HMQGGRYEFA MERAEADREF HFAGFENVKA
     KTLKWPLSVI RISSPERGGI QRLAAKIFDA WSAYSDKSVT IFAETEKGKH NAITPIARRR
     GGEYELDLVL RNNLTTPERP MGLYHPRPEY HNIKKENIGL IEVMGLAVLP SRLKKELAAV
     ADAVLAGKNI ADIPETAKHA AWFESFRGSY DITPENINDI LLRETGNTFV RVLCDCGVFK
     RDEKGIAAFD RFIDFVNKF
//
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