ID E4LC29_9FIRM Unreviewed; 355 AA.
AC E4LC29;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=HMPREF9199_1342 {ECO:0000313|EMBL:EFR60958.1};
OS Veillonella sp. oral taxon 158 str. F0412.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR60958.1, ECO:0000313|Proteomes:UP000003565};
RN [1] {ECO:0000313|EMBL:EFR60958.1, ECO:0000313|Proteomes:UP000003565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0412 {ECO:0000313|EMBL:EFR60958.1,
RC ECO:0000313|Proteomes:UP000003565};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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:EFR60958.1}.
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DR EMBL; AENU01000007; EFR60958.1; -; Genomic_DNA.
DR AlphaFoldDB; E4LC29; -.
DR STRING; 879309.HMPREF9199_1342; -.
DR eggNOG; COG4185; Bacteria.
DR OrthoDB; 9792687at2; -.
DR Proteomes; UP000003565; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR Gene3D; 1.10.8.130; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR035569; Antitoxin_epsilon/PezA_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010488; Zeta_toxin_domain.
DR Pfam; PF06414; Zeta_toxin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 129..314
FT /note="Zeta toxin"
FT /evidence="ECO:0000259|Pfam:PF06414"
SQ SEQUENCE 355 AA; 39885 MW; 2F87D7A3D1C4CB3E CRC64;
MNVVEQYNLT LQIEVLKEQS GETLARLCNL VEGSGTSDCV ELLKEYSHIV NTELYLATSI
HELDILKLDM VKLKNTIKES IAQASHDISD VKAVKETGDV QAIESYSSED FDKALERTID
FLTFNKNISS TPRAVILGGQ SGAGKTTIHR VKMLESKGNY IVIDGDTYRA QHPYFRELQE
KYGVDSVDYT KMFAGKMVEA VIDKLSSLKY NLIIEGTLRS AAVPINTAIL LKSKGYTVDF
CLIATKPELS YLTTQLRYLE MMIVDPLQAR ATPKDHHDGI VKSLVYNSNE LEQSGLFESI
QVYKRDLEQV YNSKLCTESV GTVVDKILFG PWTSDEYALL EVSKSQEQEL RAKLH
//
