GNA1_CAEEL
ID GNA1_CAEEL Reviewed; 165 AA.
AC Q17427;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000250|UniProtKB:Q96EK6};
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
GN Name=gna-1; ORFNames=B0024.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9867860; DOI=10.1074/jbc.274.1.424;
RA Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.;
RT "Saccharomyces cerevisiae GNA1, an essential gene encoding a novel
RT acetyltransferase involved in UDP-N-acetylglucosamine synthesis.";
RL J. Biol. Chem. 274:424-429(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-
CC acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q96EK6};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 1/2.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB017628; BAA36497.1; -; mRNA.
DR EMBL; Z71178; CAA94884.1; -; Genomic_DNA.
DR PIR; T37319; T37319.
DR RefSeq; NP_505654.1; NM_073253.5.
DR PDB; 4AG7; X-ray; 1.55 A; A/B=1-165.
DR PDB; 4AG9; X-ray; 1.76 A; A/B=1-165.
DR PDBsum; 4AG7; -.
DR PDBsum; 4AG9; -.
DR AlphaFoldDB; Q17427; -.
DR SMR; Q17427; -.
DR BioGRID; 44467; 7.
DR DIP; DIP-25958N; -.
DR IntAct; Q17427; 4.
DR STRING; 6239.B0024.12; -.
DR EPD; Q17427; -.
DR PaxDb; Q17427; -.
DR PeptideAtlas; Q17427; -.
DR EnsemblMetazoa; B0024.12.1; B0024.12.1; WBGene00001646.
DR GeneID; 179437; -.
DR KEGG; cel:CELE_B0024.12; -.
DR UCSC; B0024.12; c. elegans.
DR CTD; 179437; -.
DR WormBase; B0024.12; CE05156; WBGene00001646; gna-1.
DR eggNOG; KOG3396; Eukaryota.
DR GeneTree; ENSGT00390000008666; -.
DR HOGENOM; CLU_072095_2_0_1; -.
DR InParanoid; Q17427; -.
DR OMA; NQRYDWI; -.
DR OrthoDB; 1479446at2759; -.
DR PhylomeDB; Q17427; -.
DR BRENDA; 2.3.1.4; 1045.
DR Reactome; R-CEL-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SignaLink; Q17427; -.
DR UniPathway; UPA00113; UER00529.
DR PRO; PR:Q17427; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001646; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1.
DR PANTHER; PTHR13355; PTHR13355; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..165
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000074556"
FT DOMAIN 22..165
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 114..119
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 135..136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:4AG7"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:4AG7"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4AG7"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:4AG7"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4AG7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4AG7"
SQ SEQUENCE 165 AA; 18459 MW; 215C7CD7A6165BB4 CRC64;
MSHIFDASVL APHIPSNLPD NFKVRPLAKD DFSKGYVDLL SQLTSVGNLD QEAFEKRFEA
MRTSVPNYHI VVIEDSNSQK VVASASLVVE MKFIHGAGSR GRVEDVVVDT EMRRQKLGAV
LLKTLVSLGK SLGVYKISLE CVPELLPFYS QFGFQDDCNF MTQRF
