GALT_STRMU
ID GALT_STRMU Reviewed; 491 AA.
AC P96994;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12;
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=galT; OrderedLocusNames=SMU_887;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=8973358; DOI=10.1016/s0378-1119(96)00434-9;
RA Ajdic D., Sutcliffe I.C., Russell R.R.B., Ferretti J.J.;
RT "Organization and nucleotide sequence of the Streptococcus mutans galactose
RT operon.";
RL Gene 180:137-144(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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 -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 2 family. {ECO:0000305}.
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DR EMBL; U21942; AAB49737.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58601.1; -; Genomic_DNA.
DR PIR; JC5312; JC5312.
DR RefSeq; NP_721295.1; NC_004350.2.
DR RefSeq; WP_002352255.1; NC_004350.2.
DR AlphaFoldDB; P96994; -.
DR STRING; 210007.SMU_887; -.
DR PRIDE; P96994; -.
DR EnsemblBacteria; AAN58601; AAN58601; SMU_887.
DR KEGG; smu:SMU_887; -.
DR PATRIC; fig|210007.7.peg.794; -.
DR eggNOG; COG4468; Bacteria.
DR HOGENOM; CLU_047799_0_0_9; -.
DR OMA; IVDWPMS; -.
DR PhylomeDB; P96994; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002512; 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; PTHR39191; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF006005; GalT_BS; 1.
DR TIGRFAMs; TIGR01239; galT_2; 1.
DR PROSITE; PS01163; GAL_P_UDP_TRANSF_II; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..491
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169913"
FT CONFLICT 27
FT /note="S -> R (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> R (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> Y (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="N -> D (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="R -> H (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="I -> V (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="I -> V (in Ref. 1; AAB49737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55445 MW; 25A5981BB50BF9A0 CRC64;
MTALLDTFVS KIIENSDYAE LDATYLSNRI LALVGEDNAQ QDTNQSNLIA LKDELVDLAV
VNGKVGDLAE EKDCLGAELM NFITPIPSQV NKAFWDTNAK SPQKAIKDFY ELSKRNNYIK
VTAIAKNIAF TTSSVYGDID ITINLSKPEK DPKAIAAAKL AKTSNYPKCQ LCMENEGYQG
RINYPARANH RIIRMNLGDE KWGFQYSPYA YFNEHCIFLN TEHVPMVISQ NTFRQLLDIV
DIFPGYFAGS NSDLPIVGGS ILSHNHYQGG RHIFPMEIAE LDSVFRFKDF PDVTAGIVKW
PMSVIRLRGA NKYSLVELAE IIRLAWRNYS DDTMNILAFT GDTPHHTVTP IARKRDGQFE
LDIVLRDNHT TAEYPDGVYH PHIDVQHIKK ENIGLIEVMG LAILPPRLKK ELAEVEKYVL
NQYNEMADYH KDWADAIKAS HPETSSETVS EIVKQAVGRT FVRVLEDAGV YKRNRQGQAA
FMRFVESIGV K