ID H6LBH2_ACEWD Unreviewed; 537 AA.
AC H6LBH2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative kinase {ECO:0000313|EMBL:AFA48927.1};
GN OrderedLocusNames=Awo_c21520 {ECO:0000313|EMBL:AFA48927.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA48927.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA48927.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
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DR EMBL; CP002987; AFA48927.1; -; Genomic_DNA.
DR RefSeq; WP_014356527.1; NC_016894.1.
DR AlphaFoldDB; H6LBH2; -.
DR STRING; 931626.Awo_c21520; -.
DR KEGG; awo:Awo_c21520; -.
DR eggNOG; COG1461; Bacteria.
DR HOGENOM; CLU_017496_1_0_9; -.
DR OrthoDB; 9760324at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR033470; FakA-like_C.
DR InterPro; IPR048394; FakA-like_M.
DR InterPro; IPR019986; YloV-like.
DR NCBIfam; TIGR03599; YloV; 1.
DR PANTHER; PTHR33434; DEGV DOMAIN-CONTAINING PROTEIN DR_1986-RELATED; 1.
DR PANTHER; PTHR33434:SF4; PHOSPHATASE PROTEIN-RELATED; 1.
DR Pfam; PF02734; Dak2; 1.
DR Pfam; PF13684; FakA-like_C; 1.
DR Pfam; PF21645; FakA-like_M; 1.
DR SMART; SM01121; Dak1_2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFA48927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007177};
KW Transferase {ECO:0000313|EMBL:AFA48927.1}.
FT DOMAIN 9..201
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 537 AA; 58222 MW; A5DFD76B9E0F957B CRC64;
MKSQTIDGEM LVKMFRYGAK NLEINKRIVD ELNVFPVPDG DTGTNMSLTF SHSVSEFDKI
EKLNVYSVAK SASSGALIGA RGNSGVILSQ LLRGFAEGCK VNEELDIPAL ANALKLAADV
AYKAVMKPTE GTILTVAREM GEFAVEKYNT YNDFEAFITD VINHGKATLA KTPDLLPVLK
EAGVVDAGGQ GLICIAEGAL KALLNEELGV EIEVKSGNLD KFVDDSHMRP EDITFGYCTE
FIIKEASEVD EGELRTYLNT IGDSVVVVKD DAIVKVHVHT DNPGLAIERG GSLGGLIRIK
IDNMRDQFLS KGTNANEAIV PYGFIAVSPG AGVTTLFKDL GVTRIITGGQ TMNPSTQDFL
NEVDKLNAET IFIFPNNSNI IMAAQQASEI SDKQVHVISS KNIPQCIAAM LAFSPEIEAD
ENVAGMSEAI KHVATGEVTY AVRDTKINGL KIKKSNVIGL SAGEIKFTGK NIKQVTEDLL
NDMVNEDSEL ISIYYGEEVS EKDAALLVEE LSETFEDCDV EMHYGGQPLY YYIVSVE
//