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Database: UniProt
Entry: E3E6D9_PAEPS
LinkDB: E3E6D9_PAEPS
Original site: E3E6D9_PAEPS 
ID   E3E6D9_PAEPS            Unreviewed;       547 AA.
AC   E3E6D9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   ECO:0000313|EMBL:ADO58008.1};
GN   ORFNames=PPSC2_18905 {ECO:0000313|EMBL:ADO58008.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58008.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO58008.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO58008.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO58008.1; -; Genomic_DNA.
DR   RefSeq; WP_013372585.1; NC_014622.2.
DR   AlphaFoldDB; E3E6D9; -.
DR   STRING; 1406.LK13_06115; -.
DR   KEGG; ppm:PPSC2_18905; -.
DR   PATRIC; fig|886882.15.peg.4052; -.
DR   eggNOG; COG4468; Bacteria.
DR   HOGENOM; CLU_047799_0_0_9; -.
DR   OrthoDB; 2293at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000006868; Chromosome.
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   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:UP000006868};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00571}.
FT   DOMAIN          99..263
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          279..463
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
SQ   SEQUENCE   547 AA;  61857 MW;  D690956B7DE4991D CRC64;
     MSERQSVDKD QDRELSRHLA HDIDETVQQS ALYAVEQLVA FAQKKGLIGL QDTDYSRNLL
     LEQFGFSEPY SGGEAGGIIA PEALQPVLNV LIDYGFAIGL IPENTDTYRD LLDSKIMGQL
     MARPSEVIRD FHQTEAELGI EAATDAFYQL SIDSNYIRMD RVASNVYWNQ STPYGDMEIT
     INLSKPEKSP KEIAMAKLLP PPVYPKCQLC RENVGYAGRV NHPSRQNLRI IPVELNGEPW
     FFQYSPYVYY NEHCIVFHHD HVPMKLTKDT LRRLLAFTKA FPHYFIGSNA DLPIVGGSIL
     THDHFQGGRH TFPIEKAGVD GVYHNEAFPQ VTAGIVNWPM SVIRFTSTDA EALLEAGNAA
     FEAWKGYSDP SVDVLSHTEL EGETIPHNTV TPIVRRDSEG RYQMDLVLRN NRTSEEYPEG
     IFHPHREMHH IKKENIGLIE VMGLAILPGR LKDELDGIAD ILCGNDELAV AMQQEEHPLF
     KHADWIYQLN TRFGRLSDKE TAVRIVQNEV GLKFSEILEH AGVYKRNPSG QQAFGRFMKQ
     LGYTLGE
//
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