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Database: UniProt
Entry: W2VGP8_9FIRM
LinkDB: W2VGP8_9FIRM
Original site: W2VGP8_9FIRM 
ID   W2VGP8_9FIRM            Unreviewed;       197 AA.
AC   W2VGP8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=HMPREF1495_2393 {ECO:0000313|EMBL:ETO97486.1};
OS   Lachnoanaerobaculum sp. MSX33.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnoanaerobaculum.
OX   NCBI_TaxID=936596 {ECO:0000313|EMBL:ETO97486.1, ECO:0000313|Proteomes:UP000018910};
RN   [1] {ECO:0000313|EMBL:ETO97486.1, ECO:0000313|Proteomes:UP000018910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSX33 {ECO:0000313|EMBL:ETO97486.1,
RC   ECO:0000313|Proteomes:UP000018910};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) 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:ETO97486.1}.
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DR   EMBL; AZXX01000060; ETO97486.1; -; Genomic_DNA.
DR   RefSeq; WP_034212674.1; NZ_AZXX01000060.1.
DR   AlphaFoldDB; W2VGP8; -.
DR   PATRIC; fig|936596.3.peg.1023; -.
DR   eggNOG; COG4185; Bacteria.
DR   OrthoDB; 9791543at2; -.
DR   Proteomes; UP000018910; 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   PANTHER; PTHR39206; SLL8004 PROTEIN; 1.
DR   PANTHER; PTHR39206:SF1; SLL8004 PROTEIN; 1.
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          2..164
FT                   /note="Zeta toxin"
FT                   /evidence="ECO:0000259|Pfam:PF06414"
SQ   SEQUENCE   197 AA;  22424 MW;  6B8E02A2540B91E4 CRC64;
     MPTYTIFAGV NGAGKSTLYS ILLQENHDFG VRVNSDEIVI SNSGDWRNKS DQAKAMKMAV
     KIIKDCMNKC ISFNQETTLT GRSMLNNILK AKKLGYKIIM NYVGLNSPEL AIQRVAHRVS
     MGGHGIPEED IKRRYYVSLS KLKELMSLID ELYIYDNSKH MKLVAKEIAG CRTLLENNCL
     WLSSSHLFDR YTNEFML
//
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