ID E8UQZ7_THEBF Unreviewed; 323 AA.
AC E8UQZ7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000313|EMBL:ADV80567.1};
DE EC=2.7.7.12 {ECO:0000313|EMBL:ADV80567.1};
GN OrderedLocusNames=Thebr_2052 {ECO:0000313|EMBL:ADV80567.1};
OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS AKO-1) (Thermoanaerobacter finnii).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV80567.1, ECO:0000313|Proteomes:UP000002062};
RN [1] {ECO:0000313|EMBL:ADV80567.1, ECO:0000313|Proteomes:UP000002062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC {ECO:0000313|Proteomes:UP000002062};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL Submitted (JAN-2011) 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};
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000256|ARBA:ARBA00010951}.
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DR EMBL; CP002466; ADV80567.1; -; Genomic_DNA.
DR RefSeq; WP_012269710.1; NC_014964.1.
DR AlphaFoldDB; E8UQZ7; -.
DR KEGG; tbo:Thebr_2052; -.
DR HOGENOM; CLU_029960_1_0_9; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002062; 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; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR005850; GalP_Utransf_C.
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; PF02744; GalP_UDP_tr_C; 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 Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000808-3};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ADV80567.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADV80567.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT DOMAIN 3..170
FT /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01087"
FT DOMAIN 180..288
FT /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02744"
FT ACT_SITE 160
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
SQ SEQUENCE 323 AA; 37176 MW; 909EACAC9C1685C5 CRC64;
MSEIRYDLIT GKRVIIATER GKRPHDFNVN YEGKKNNNTC PFCPMNEEMT PPTLVEIKDK
KGNWLVRGFE NKFAAVNRDL KSFEVPSLYK AEYGYGVAEV IVESPEHDVT FGSLSLGQMQ
KVFMAIIERY KKIAQDDKIK YIQVFKNFGA RGGASLEHGH WQIIAISFIP DVVEKEVTGT
QEYIKKKGKC PYCEIVKYEK EEGKRIIAEN ESFIIIAPYA SQYPYESWVI PKEHQERFEE
LREGNIASLT EILKPLIEKY EKEFNLPPYN IVIHTLPISD IRNYHWHIEI IPRLTVAAGF
ELGTGVYINP VPPELAASVL RIE
//
