ID E8LFG6_9FIRM Unreviewed; 206 AA.
AC E8LFG6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=UDP-N-acetylglucosamine kinase {ECO:0000256|ARBA:ARBA00011963};
DE EC=2.7.1.176 {ECO:0000256|ARBA:ARBA00011963};
DE AltName: Full=UDP-N-acetylglucosamine kinase {ECO:0000256|ARBA:ARBA00032897};
GN ORFNames=HMPREF9443_01607 {ECO:0000313|EMBL:EFY04421.1};
OS Phascolarctobacterium succinatutens YIT 12067.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Phascolarctobacterium.
OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY04421.1, ECO:0000313|Proteomes:UP000004923};
RN [1] {ECO:0000313|EMBL:EFY04421.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY04421.1};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UDP-N-acetyl-alpha-D-glucosamine = ADP + H(+) + UDP-N-
CC acetyl-alpha-D-glucosamine 3'-phosphate; Xref=Rhea:RHEA:32671,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:64353, ChEBI:CHEBI:456216; EC=2.7.1.176;
CC Evidence={ECO:0000256|ARBA:ARBA00000912};
CC -!- SIMILARITY: Belongs to the zeta toxin family.
CC {ECO:0000256|ARBA:ARBA00009104}.
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:EFY04421.1}.
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DR EMBL; AEVN01000079; EFY04421.1; -; Genomic_DNA.
DR AlphaFoldDB; E8LFG6; -.
DR eggNOG; COG0645; Bacteria.
DR HOGENOM; CLU_088583_0_0_9; -.
DR OrthoDB; 9776406at2; -.
DR Proteomes; UP000004923; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007530; Aminoglycoside_adenylylTfrase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010488; Zeta_toxin_domain.
DR Pfam; PF04439; Adenyl_transf; 1.
DR Pfam; PF06414; Zeta_toxin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:EFY04421.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004923};
KW Transferase {ECO:0000313|EMBL:EFY04421.1}.
FT DOMAIN 6..46
FT /note="Zeta toxin"
FT /evidence="ECO:0000259|Pfam:PF06414"
SQ SEQUENCE 206 AA; 24284 MW; 93FA7B3D168FB6BC CRC64;
MNQGRIIVIT GAPGTGKTTT ASAVAKESDL EKSVHMHTDD FYHYHVRKPS AREYDDCCNE
FWNVTPYVIK GLCRKEILFA IDHFNQIVRH ELLRMISWKV GIETGFKLSV GKNYKFIERY
ISEDLWEKLL STYRMDSYEN IWEALFLCHQ LFRAVSGEVA ERLHYAYPEY DRNITKYTRD
MYKKYTGKTG CLDSTYAADI EERREQ
//