ID Q63F38_BACCZ Unreviewed; 583 AA.
AC Q63F38;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:AAU19373.1};
DE EC=2.7.1.29 {ECO:0000313|EMBL:AAU19373.1};
GN Name=dhaL {ECO:0000313|EMBL:AAU19373.1};
GN OrderedLocusNames=BCE33L0870 {ECO:0000313|EMBL:AAU19373.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU19373.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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DR EMBL; CP000001; AAU19373.1; -; Genomic_DNA.
DR AlphaFoldDB; Q63F38; -.
DR KEGG; bcz:BCE33L0870; -.
DR PATRIC; fig|288681.22.peg.4705; -.
DR OMA; TALNMNG; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
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; IPR012736; DhaK_1.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR012737; DhaK_L_YcgS.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR NCBIfam; TIGR02365; dha_L_ycgS; 1.
DR NCBIfam; TIGR02363; dhaK1; 1.
DR PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR PANTHER; PTHR28629:SF4; TRIOKINASE/FMN CYCLASE; 1.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAU19373.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAU19373.1}.
FT DOMAIN 7..327
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 371..580
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 583 AA; 62357 MW; 65BB818851B8E21A CRC64;
MKKIINKPET LVMEMCNGMV MAHPELELLK KYKVIKKKEM NENKVTLISG GGSGHEPAHA
GLVGKGMLDA AVCGDVFASP SQIQVYQAIK ETASKKGTLL IIKNYSGDIM NFKNGAHLAT
EDGIEVDYVK VDDDIAVEDS LYTVGRRGVA GVILVHKIAG AAAEAGMDLG AVKAVAEKAA
ANVRTIGLAL TSCTVPASGS PTFTLAEDEM EYGVGIHGEP GIKREKMLSA DELANRMTND
LVKDLGVKDG EEIALLVNGF GGTPLQELYL FNNAVTRELA ARNIKINRVF VGNYMTSIDM
AGMSLTVMKL DGELKTLLSK ECNTPAFKVD GPVESVEYVN VLEETEEKEV SFELETAEEH
AVIKDNVITL NNMIYLVDKM SDIIIKNEVP FCELDTHAGD GDFGMSVAKG FKQLKREWHS
IVEQENVTIG SFLDGCSMII MEHCGGASGP IWGGAFRAAS KAAGEKRELT VKEFAEMLQA
ALQGIQSIGE RSFGRGAVVG DKTLVDALAP CVDSWLASAS DEVDMKTAFE KGAEAAVKGA
EYTKEIVARM GRAGTVGERS LGYPDAGAHA LGVIFTEIAG SLK
//