ID Q5FAE1_NEIG1 Unreviewed; 413 AA.
AC Q5FAE1;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=UDP-N-acetylgalactosaminyltransferase {ECO:0000313|EMBL:AAW88846.1};
GN ORFNames=NGO_0085 {ECO:0000313|EMBL:AAW88846.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88846.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4M98, ECO:0007829|PDB:4M99}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 197-403 IN COMPLEX WITH
RP ACETYL-COA.
RX PubMed=24064219; DOI=10.1074/jbc.M113.510560;
RA Morrison M.J., Imperiali B.;
RT "Biochemical analysis and structure determination of bacterial
RT acetyltransferases responsible for the biosynthesis of UDP-N,N'-
RT diacetylbacillosamine.";
RL J. Biol. Chem. 288:32248-32260(2013).
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000256|ARBA:ARBA00006464}.
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DR EMBL; AE004969; AAW88846.1; -; Genomic_DNA.
DR RefSeq; WP_003704933.1; NC_002946.2.
DR RefSeq; YP_207258.1; NC_002946.2.
DR PDB; 4M98; X-ray; 1.67 A; A=197-403.
DR PDB; 4M99; X-ray; 2.60 A; A/B/C=196-403.
DR PDBsum; 4M98; -.
DR PDBsum; 4M99; -.
DR AlphaFoldDB; Q5FAE1; -.
DR SMR; Q5FAE1; -.
DR STRING; 242231.NGO_0085; -.
DR KEGG; ngo:NGO_0085; -.
DR PATRIC; fig|242231.10.peg.112; -.
DR HOGENOM; CLU_054372_0_0_4; -.
DR BRENDA; 2.3.1.203; 3590.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03360; LbH_AT_putative; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR020019; AcTrfase_PglD-like.
DR InterPro; IPR003362; Bact_transf.
DR InterPro; IPR041561; PglD_N.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR03570; NeuD_NnaD; 1.
DR PANTHER; PTHR30576; COLANIC BIOSYNTHESIS UDP-GLUCOSE LIPID CARRIER TRANSFERASE; 1.
DR PANTHER; PTHR30576:SF8; UNDECAPRENYL-PHOSPHATE GALACTOSE PHOSPHOTRANSFERASE; 1.
DR Pfam; PF02397; Bac_transf; 1.
DR Pfam; PF17836; PglD_N; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4M98, ECO:0007829|PDB:4M99};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000535};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..180
FT /note="Bacterial sugar transferase"
FT /evidence="ECO:0000259|Pfam:PF02397"
FT DOMAIN 201..276
FT /note="PglD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17836"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT BINDING 342
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT BINDING 351
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT BINDING 360
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT BINDING 363
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT BINDING 368
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT BINDING 381
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT BINDING 401
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0007829|PDB:4M99"
FT SITE 334
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
SQ SEQUENCE 413 AA; 44266 MW; 81FD30120CBDB73A CRC64;
MSKAVKRLFD IIASASGLIV LSPVFLVLIY LIRKNLGSPV FFIRERPGKD GKPFKMVKFR
SMRDALDSDG IPLPDSERLT DFGKKLRATS LDELPELWNV LKGEMSLVGP RPLLMQYLPL
YNKFQNRRHE MKPGITGWAQ VNGRNALSWD EKFSCDVWYT DNFSFWLDMK ILFLTVKKVL
IKEGISAQGE ATMPPFAGNR KLAVIGAGGH GKVVAELAAA LGTYGEIVFL DDRTQGSVNG
FPVIGTTLLL ENSLSPEQFD ITVAVGNNRI RRQITENAAA LGFKLPVLIH PDATVSPSAI
IGQGSVVMAK AVVQAGSVLK DGVIVNTAAT VDHDCLLDAF VHISPGAHLS GNTRIGEESR
IGTGACSRQQ TTVGSGVTAG AGAVIVCDIP DGMTVAGNPA KPLTGKNPKT GTA
//
