GALT_BIFL2
ID GALT_BIFL2 Reviewed; 515 AA.
AC E8MF11; A7BJ82;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00571};
DE Short=Gal-1-P uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00571};
DE EC=2.7.7.12 {ECO:0000255|HAMAP-Rule:MF_00571};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00571};
GN Name=galT {ECO:0000255|HAMAP-Rule:MF_00571}; Synonyms=lnpC;
GN OrderedLocusNames=BLLJ_1621;
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=17720833; DOI=10.1128/aem.01425-07;
RA Nishimoto M., Kitaoka M.;
RT "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-
RT biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum.";
RL Appl. Environ. Microbiol. 73:6444-6449(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
CC -!- FUNCTION: Transfers the UMP unit from UDP-glucose (UDP-Glc) to Gal1P.
CC Can also transfer the UMP unit to GlcNAc1P and GalNAc1P. Involved in
CC the general galactose metabolism, and also involved in the lacto-N-
CC biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is
CC important for host intestinal colonization by bifidobacteria.
CC {ECO:0000269|PubMed:17720833}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00571, ECO:0000269|PubMed:17720833};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00571, ECO:0000269|PubMed:17720833}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00571}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 2 family. {ECO:0000255|HAMAP-Rule:MF_00571}.
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DR EMBL; AB303839; BAF73926.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ67288.1; -; Genomic_DNA.
DR RefSeq; WP_007052335.1; NC_015067.1.
DR AlphaFoldDB; E8MF11; -.
DR KEGG; blm:BLLJ_1621; -.
DR HOGENOM; CLU_047799_0_0_11; -.
DR OMA; IVDWPMS; -.
DR UniPathway; UPA00214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
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; PTHR39191; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..515
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000424072"
FT CONFLICT 471
FT /note="D -> N (in Ref. 1; BAF73926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56723 MW; CBF4C1D33AAED657 CRC64;
MNDQLTEVYA SIDALIDYAL AHLDLDPRNA DWTRNQIFAL FRLDSYPGPK TTTSAASVSD
VVQDIVGSRS QAPYGEKTPD PLLAAFRAAA TTAGLFKPEE GPAYADTIMG ILSANPADLD
DRFLLVEHRD GGMAAMQWFY DYCVANNYVK RAQLDRNPRF DSHGLTVTIN LAKPEFKNMK
KAAAGNAVAG GYPKCTICHE NEGFAGRDKR TLRTLPVTLG GESWFWQFSP YGYFDQHGIC
VNTDHTPMHV DRDTFGHLLD FVDRFPGYFL GCNAALPRIG GSVLAHDHYQ GGGELLPMHK
AATWAAFTLA DYPDAVVEIL DWPGTAVRVV SKSRQSIIDV SDIIREAWVG YDDAANGIAS
HDADGNRQSA LSPSAIITER GYEMSLIFRN NAISDEYPEG IFHAHPEYWP VKQEPIGLIE
AQGLFILPGR LVDQLGIVEE ALAEGRDLPD EVSEFSLEWG ELAETLAGNH DREAIRQAVH
DELGSVCYRI LGNTAVFKQK ATTQTFLESL GFAAR