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Database: UniProt
Entry: K9GGV5_PEND1
LinkDB: K9GGV5_PEND1
Original site: K9GGV5_PEND1 
ID   K9GGV5_PEND1            Unreviewed;       384 AA.
AC   K9GGV5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00016340, ECO:0000256|RuleBase:RU000506};
DE            EC=2.7.7.12 {ECO:0000256|ARBA:ARBA00012384, ECO:0000256|RuleBase:RU000506};
GN   ORFNames=PDIP_16450 {ECO:0000313|EMBL:EKV20442.1};
OS   Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV20442.1, ECO:0000313|Proteomes:UP000009886};
RN   [1] {ECO:0000313|Proteomes:UP000009886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001107,
CC         ECO:0000256|RuleBase:RU000506};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000808-4};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR000808-4};
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   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU000506}.
CC   -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC       type 1 family. {ECO:0000256|ARBA:ARBA00010951,
CC       ECO:0000256|RuleBase:RU000506}.
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:EKV20442.1}.
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DR   EMBL; AKCU01000116; EKV20442.1; -; Genomic_DNA.
DR   RefSeq; XP_014537814.1; XM_014682328.1.
DR   AlphaFoldDB; K9GGV5; -.
DR   GeneID; 26229968; -.
DR   KEGG; pdp:PDIP_16450; -.
DR   HOGENOM; CLU_029960_0_0_1; -.
DR   OrthoDB; 1428870at2759; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000009886; Unassembled WGS sequence.
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   CDD; cd00608; GalT; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 2.
DR   InterPro; IPR001937; GalP_UDPtransf1.
DR   InterPro; IPR019779; GalP_UDPtransf1_His-AS.
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; PTHR11943; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR11943:SF1; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 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.
DR   PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000506};
KW   Galactose metabolism {ECO:0000256|RuleBase:RU000506};
KW   Iron {ECO:0000256|PIRSR:PIRSR000808-4};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000808-3};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000506};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000506};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000808-3}.
FT   DOMAIN          6..208
FT                   /note="Galactose-1-phosphate uridyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01087"
FT   DOMAIN          216..373
FT                   /note="Galactose-1-phosphate uridyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02744"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Tele-UMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-1"
FT   BINDING         27..30
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         60
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         76..77
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         185
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         191..193
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-3"
FT   BINDING         200
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         314
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         331
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         333
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-4"
FT   BINDING         346..347
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         351..352
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
FT   BINDING         358
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000808-2"
SQ   SEQUENCE   384 AA;  43838 MW;  AD13453A44839ED4 CRC64;
     MENVLDDISH RRYNPLRGSS ILVSPHRTKR PWQGAQESPS KTTLPNYDPK CYLCPGNKRA
     QGDTNPNYKS TFVFVNDYSA VKEEQAAYEP SYQDELESRF LKAEPVSGKC YVLTFSSAHN
     LTLADLAPHE IMPVINAWTE IYTVHLSPTW PLAKHAPAKT LLPTSPSSSI TKPKEQYRYM
     QIFENKGAAM GCSNPHPHGQ VWTTSSMPEE PATEMNQLIK YRQQHGGSHL LEDYAELESR
     KQERVVFENE AFLVVCPWWA TWPFETMIVS RNHKRALVDL SEADKMLLAE AIAETTRRYD
     NLFETHFPYS MGIHQAPLDG TEEEIEASYL HLHFYPPLLR SATVRKFLVG YELMAEPQRD
     ITPEQAAAKL RACGGELYRK KIDS
//
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