ID   A0A957VW00_9CHLR        Unreviewed;       332 AA.
AC   A0A957VW00;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   13-SEP-2023, entry version 4.
DE   SubName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000313|EMBL:MCB0164658.1};
GN   Name=galT {ECO:0000313|EMBL:MCB0164658.1};
GN   ORFNames=KDI79_10545 {ECO:0000313|EMBL:MCB0164658.1};
OS   Anaerolineae bacterium.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=2052143 {ECO:0000313|EMBL:MCB0164658.1, ECO:0000313|Proteomes:UP000740037};
RN   [1] {ECO:0000313|EMBL:MCB0164658.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HKST-UBA15 {ECO:0000313|EMBL:MCB0164658.1};
RA   Zhang T.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MCB0164658.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HKST-UBA15 {ECO:0000313|EMBL:MCB0164658.1};
RX   PubMed=34615557;
RA   Wang Y., Ye J., Ju F., Liu L., Boyd J.A., Deng Y., Parks D.H., Jiang X.,
RA   Yin X., Woodcroft B.J., Tyson G.W., Hugenholtz P., Polz M.F., Zhang T.;
RT   "Successional dynamics and alternative stable states in a saline activated
RT   sludge microbial community over 9 years.";
RL   Microbiome 9:0-0(2021).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000808-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000808-3};
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC       type 1 family. {ECO:0000256|ARBA:ARBA00010951}.
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:MCB0164658.1}.
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DR   EMBL; JAGRCC010000296; MCB0164658.1; -; Genomic_DNA.
DR   Proteomes; UP000740037; Unassembled WGS sequence.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:InterPro.
DR   Gene3D; 3.30.428.10; HIT-like; 2.
DR   InterPro; IPR001937; GalP_UDPtransf1.
DR   InterPro; IPR005849; GalP_Utransf_N.
DR   InterPro; IPR036265; HIT-like_sf.
DR   NCBIfam; TIGR00209; galT_1; 1.
DR   PANTHER; PTHR42763; ADP-GLUCOSE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42763:SF2; ADP-GLUCOSE PHOSPHORYLASE; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF000808; GalT; 1.
DR   SUPFAM; SSF54197; HIT-like; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000808-3};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:MCB0164658.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT   DOMAIN          3..175
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   ACT_SITE        165
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
SQ   SEQUENCE   332 AA;  38539 MW;  B3D00C4BAD22E580 CRC64;
     MPELRQNMAT KEWVIIATER AERPDGFIQS ESLSITGDEP TFDPTCPFCP GNEELDLEIE
     CWPDRDVWQT RVVHNKFPAL SKDDSLTRKF DGVQRWISGA GHHEIVVDHP KHNTTWALMS
     PPEIMAVLEM FQRRGWRIHE DERVEQIIYF KNHGYRAGAS LKHPHSQIIA LPIVPTNIRQ
     RLEEARRYFD DYGQNVFRVM VENELARGER ILVESKHFVA FVLYAAPAPF HTWIIPRQQS
     ISFLYAQPDE LADLAEVLVN VLRRLYFGLR DPSYNLIIRS APVKEISNDY YQWYITIVPR
     LNYAAGFELG SGMFINPTLP EGCADFLRKV KI
//