ID L1N2I6_9FIRM Unreviewed; 363 AA.
AC L1N2I6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 03-MAY-2023, entry version 30.
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=HMPREF9163_01334 {ECO:0000313|EMBL:EKX97575.1};
OS Selenomonas sp. oral taxon 138 str. F0429.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=1127695 {ECO:0000313|EMBL:EKX97575.1, ECO:0000313|Proteomes:UP000010434};
RN [1] {ECO:0000313|EMBL:EKX97575.1, ECO:0000313|Proteomes:UP000010434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0429 {ECO:0000313|EMBL:EKX97575.1,
RC ECO:0000313|Proteomes:UP000010434};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX97575.1}.
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DR EMBL; AMEO01000078; EKX97575.1; -; Genomic_DNA.
DR AlphaFoldDB; L1N2I6; -.
DR STRING; 1127695.HMPREF9163_01334; -.
DR PATRIC; fig|1127695.3.peg.1191; -.
DR eggNOG; COG4185; Bacteria.
DR HOGENOM; CLU_762670_0_0_9; -.
DR OrthoDB; 9792687at2; -.
DR Proteomes; UP000010434; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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}.
FT DOMAIN 132..318
FT /note="Zeta toxin"
FT /evidence="ECO:0000259|Pfam:PF06414"
SQ SEQUENCE 363 AA; 40933 MW; 5E97778272CFA3B2 CRC64;
MQHEQLALDY EVTEQKEALY EAIAALLADA LRQTEDAETH ARTLLYEALC RMWNTLLGTT
YRTREEIAML HGAYGLARDL LAGMQDDDTP ARTAAPQEMN GTLRESLASV TSEEFQYQRD
ALIRILTEGR LPAAQPLAYL IAGQPGAGKT TMADLFTGAH SGNIIFISGD AYRPFHPHIA
ELRAHFGDDA VLHTQEFAGR MTEALIDALS AQGYHLIIEG TLRTQEAPLR TRELLATRGY
RVSLNLLAVP PLLSYLGTLR RYARMREFGM HPRRTPREHH DRVVRDIAAN LDALDQMHRF
DAIRLYDRTG ACLYEENQQG GSPAEALRRA MARPFSAEER DDLRRIYAPY VPEDLLDEAL
HSY
//
