ID J3K221_COCIM Unreviewed; 594 AA.
AC J3K221;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:EAS28092.3};
GN ORFNames=CIMG_09296 {ECO:0000313|EMBL:EAS28092.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS28092.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000256|ARBA:ARBA00003264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate +
CC H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216;
CC EC=2.7.1.28; Evidence={ECO:0000256|ARBA:ARBA00000031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate +
CC H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216;
CC EC=2.7.1.29; Evidence={ECO:0000256|ARBA:ARBA00001015};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004778}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000256|ARBA:ARBA00008757}.
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DR EMBL; GG704915; EAS28092.3; -; Genomic_DNA.
DR RefSeq; XP_001239675.2; XM_001239674.2.
DR AlphaFoldDB; J3K221; -.
DR STRING; 246410.J3K221; -.
DR GeneID; 4558655; -.
DR KEGG; cim:CIMG_09296; -.
DR VEuPathDB; FungiDB:CIMG_09296; -.
DR InParanoid; J3K221; -.
DR OMA; ALNMNGF; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR NCBIfam; TIGR02361; dak_ATP; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAS28092.3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..351
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 388..592
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 227
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 594 AA; 63038 MW; 876C04E89E533D0B CRC64;
MQTKHFFNDP THLVSSALRS LTLTNPSLAF DEENKIIYRR PTGDASTQPK VSIISGGGSG
HEPAFAGFVG KGLLTASVAG TIFASPSAEQ VRRAVMQRVE VSKGVLIIIM NYTGDVLNFG
MAAEKAKAAG IKTEFFAVGD DVGVGRTKGG KVGRRGIGGG ILVLKIIGAL AEAGASLSEV
YATAKLVAKN VVSLGSSLEH VHVPGRETSD ASEVIPEGEI EVGMGIHNEP GSHRVKNTLE
ELIQTMLRQL LDQDDTDRGF LKWDSPDKFV LFINNLGGVS TLELSGITAE TILQLERDYH
IKPVRTIQGT FLTSLNGMGF SISLLRLVDT RLGQGRSLLE LLDAPAEAVG WAAPIQTSTW
ESQSDATFEG RRASSVQEAP SNLKVNISVF KKAVVSGLNR LIAAESTLTR YDTIVGDGDC
GVGLKRGAEA IVSLLNNPSV PLNDDILRSL NRIISLVETT MDGTSGAIYA IFLNALAHGL
REQDSPSNSI SVTAKVWSRA LQQSLKALAK YTPAQPGDRT LIDALVPFIN KLTESGDVKA
AARAAQEGAE STKSMKASLG RSVYIGGEDE WIGKIPDPGA YGLSEFLNGL ADGI
//
