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Database: UniProt
Entry: C9RBH5_AMMDK
LinkDB: C9RBH5_AMMDK
Original site: C9RBH5_AMMDK 
ID   C9RBH5_AMMDK            Unreviewed;       341 AA.
AC   C9RBH5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000313|EMBL:ACX51602.1};
DE            EC=2.7.7.12 {ECO:0000313|EMBL:ACX51602.1};
GN   OrderedLocusNames=Adeg_0450 {ECO:0000313|EMBL:ACX51602.1};
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Ammonifex.
OX   NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX51602.1, ECO:0000313|Proteomes:UP000002620};
RN   [1] {ECO:0000313|EMBL:ACX51602.1, ECO:0000313|Proteomes:UP000002620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP001785; ACX51602.1; -; Genomic_DNA.
DR   RefSeq; WP_015738480.1; NC_013385.1.
DR   AlphaFoldDB; C9RBH5; -.
DR   STRING; 429009.Adeg_0450; -.
DR   KEGG; adg:Adeg_0450; -.
DR   eggNOG; COG1085; Bacteria.
DR   HOGENOM; CLU_029960_1_0_9; -.
DR   OrthoDB; 9769064at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000002620; Chromosome.
DR   GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
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; IPR032576; DUF4921.
DR   InterPro; IPR001937; GalP_UDPtransf1.
DR   InterPro; IPR036265; HIT-like_sf.
DR   NCBIfam; TIGR00209; galT_1; 1.
DR   PANTHER; PTHR42763; ADP-GLUCOSE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42763:SF1; UDP-GLUCOSE--HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF16268; DUF4921; 1.
DR   PIRSF; PIRSF000808; GalT; 1.
DR   SUPFAM; SSF54197; HIT-like; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000808-3};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ACX51602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002620};
KW   Transferase {ECO:0000313|EMBL:ACX51602.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000808-3}.
FT   DOMAIN          140..325
FT                   /note="DUF4921"
FT                   /evidence="ECO:0000259|Pfam:PF16268"
FT   ACT_SITE        165
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         42
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   341 AA;  39381 MW;  26D5261341A5763B CRC64;
     MPEWRKDPVV DRWVAVSTER AKRPTDYRPP LERKKQERCP LCVGHEGDTP PEVMAFRHPG
     SLPDHPGWWV RVVPNKFPAC RVEEEDIVRP HGPYQWRCGV GAHEVIVETP EHVPNLVNQS
     EGQIAEVIWA WRARLLDLRR DTRFKYIQIF KNKGSVAGAS LEHTHSQLIA LPMVPAEIQA
     ELTGVKVYRE EKGSCVFCDL WRYELEAGER VVEESSHFLC FVPYAARFPF EMWLVPKRHK
     PDFGAIEEGE VCDLAWLLKR TLYRLAQTVF DPPFNLVLHT APVNVPEPVD YHWHIEILPR
     LTIMAGFELG TGYYINPTPP EMAAAALREQ EVEERMVSHF V
//
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