ID A0A163CMV2_DIDRA Unreviewed; 842 AA.
AC A0A163CMV2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=hexokinase {ECO:0000256|ARBA:ARBA00012324};
DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
GN ORFNames=ST47_g6301 {ECO:0000313|EMBL:KZM22576.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM22576.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM22576.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM22576.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000256|ARBA:ARBA00006824}.
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:KZM22576.1}.
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DR EMBL; JYNV01000212; KZM22576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163CMV2; -.
DR STRING; 5454.A0A163CMV2; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; 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 InterPro; IPR007248; Mpv17_PMP22.
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 Pfam; PF04117; Mpv17_PMP22; 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};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..575
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 582..830
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 842 AA; 94737 MW; 05DDE05AB52EDCE3 CRC64;
MIRTPCAWAR TSSRRATQNV HAYPREPNRV TGNTTTFNLV AQRASPAHVV RRYNVTKAPT
GHKAPATATT IPGPSWLWLE PVIEPFRAYG RVQQRKPYLT QLVSSLVIYF VGDLVAQSIA
APEEKDVTEE EEERGWVQQW SEDRDWARTG RALIIGGISS IPSYKWFLWL SLNFNYSSKI
LSLTTKVVVN QILFTPIFNS YFFGMQTLLA GASFDDCVER IKHTVPTSCI NSCKIWPAVT
AFSFTYIPIQ YRSIFGGVIA IGWQTYLNLL NQRVAAQEHL EHPARQELVN ETTTATKHKN
MDVRKENGGP KQNILLDDEL LNIHRHTSAF LEIPDFIMAS AAQQHVDKES YSSRQHRSEL
KKMADLPSEL EKELDDLDTQ FWIPGEKLKE IVKRFREELD EGLAKHEQNI AMHQTWVHRL
PSGNEKGTFL TLDLGGTNLR VCEITLRGHE KEGAEKTELN QEQYKLPEEL KKGDADGLFD
FIAQELEDFV RSKGLDKKYS KDKPMPLGFT FSYPATQARI DHAVLKTWTK GFDISGVEGQ
DVARQLREKI EKRSLPIEII CVINDTVGAM IASAYNDSKT IIGAIFGTGC NAAYMASLSD
IRKIKPSDRD TIESQYGKNS KMAINCEYGA FDNAHRVLPW TKYDQQIDAD SPRPGEQAFE
KLSAGLYMGE IYRLIMLDLA ERGLVFKNQD VNKLRASYSI DTGFLSQVED DESPTFSKSR
HLFKNTLNLE PSDIEIELSR HITELVAVRG ARLCACGVAA ICTKESIAEG HVAADGSVAN
KHPKFKKRWA RALGEILDWS EAEKKEGEGP IKITSAEDGS GIGCAIIAAM ELERRGRAQN
IV
//
