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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
 
 
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