UAP1L_XENTR
ID UAP1L_XENTR Reviewed; 511 AA.
AC Q28CH3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=UDP-N-acetylhexosamine pyrophosphorylase-like protein 1;
DE EC=2.7.7.-;
GN Name=uap1l1; ORFNames=TGas075i06.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR926388; CAJ83512.1; -; mRNA.
DR RefSeq; NP_001015926.1; NM_001015926.2.
DR AlphaFoldDB; Q28CH3; -.
DR SMR; Q28CH3; -.
DR GeneID; 548680; -.
DR KEGG; xtr:548680; -.
DR CTD; 91373; -.
DR Xenbase; XB-GENE-1002718; uap1l1.
DR InParanoid; Q28CH3; -.
DR OrthoDB; 888726at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..511
FT /note="UDP-N-acetylhexosamine pyrophosphorylase-like
FT protein 1"
FT /id="PRO_0000324583"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..120
FT /note="Substrate binding"
FT MOTIF 312..313
FT /note="Substrate binding"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..120
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 131
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 205
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 231
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 386
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 57299 MW; BDC3AEE3331D98BD CRC64;
MDRSESAESA ESRRRRAEES GQGQLFRFWD ELSPAEKEAL LEQLEMLEPR ELREHCQRAR
EAYVRESSAP QRLDDRMQPV PPEFLGSVRH SGTGELERWE REGFHQIAQN KVAVLLLAGG
QGTRLGVTYP KGMYSVGLPS AKTLYQIQAE RIRRLQQLAS ERHGETCTVP WYIMTSEFTL
GPTRKFFEDH AYFGLERSDV VMFEQRMLPA VGFDGAAILE DKAKLAMAPD GNGGLYRALS
DNRILEDMEG RGIQYVHVYC VDNILVKMAD PVFIGFCVSK GADCGAKVVE KGYPAEPVGV
VCRVDGVYQV VEYSEISPET AEKRNPNGAL TFTAGNICNH FFTVPFLRAV IGSLEPRLNY
HVAIKKVPYV DNEGNLVKPT SPNGIKMEKF VFDVFQFAKN FVAFEVLREE EFSPLKNADT
ADKDTPTTAR RALLWQHYRW ARRAGTHFLD ETGSPIRDSH SISGEGDPPA VCEISPLVSY
FGEGLESYMK DKDVSSFPFV LESSDAGPVP V