ID B8LT55_TALSN Unreviewed; 490 AA.
AC B8LT55;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=TSTA_069800 {ECO:0000313|EMBL:EED23563.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED23563.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004888}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; EQ962652; EED23563.1; -; Genomic_DNA.
DR RefSeq; XP_002340950.1; XM_002340909.1.
DR AlphaFoldDB; B8LT55; -.
DR STRING; 441959.B8LT55; -.
DR GeneID; 8107329; -.
DR VEuPathDB; FungiDB:TSTA_069800; -.
DR eggNOG; KOG1369; Eukaryota.
DR InParanoid; B8LT55; -.
DR OrthoDB; 5481886at2759; -.
DR PhylomeDB; B8LT55; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 1.10.287.1250; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362007};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 26..221
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 227..467
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 490 AA; 54506 MW; 6F5302DA53F33540 CRC64;
MVGLGPRRRP SRKGSMADVP KSLLDQIKEF EDIFTVDRQK LKEVVAHFVK ELEKGLSVEG
GNIPMNVTWV FGFPTGDEQG NFLALDMGGT NLRVCEIQLT AERGEFDITQ SKYRIPEELK
TGTAEELWEY IADCLQQFIE YHHEDEELPS LPLGFTFSYP ATQEYIDHGI LQRWTKGFDI
EGVEGKDVVP PFEEVLQKRG LPIKTTALIN DTTGTLIASA YTDPEMKIGC IFGTGVNAAY
MEDAGSVPKI AHLNLPPDTP IAINCEYGAF DNEHVVLPLT QYDIIIDRDS PRPGQQAFEK
MTAGLYLGEI YRLALLDVID NKPGLIFEGQ DVSKLRKPYS LDASFLSAIE EDPFENLQET
QELLERVLGI KAVKAELELC RRLAELIGTR AARLSACGVA AICTKKKIER CHVGADGSVF
TKYPHFQARG ARALREILDW EDNEKDKVVI LPAEDGSGVG AALIAALTLK RYKEGNLVGI
KDKDSFKCFV
//
