ID W6QN81_PENRF Unreviewed; 624 AA.
AC W6QN81;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=PROQFM164_S02g001257 {ECO:0000313|EMBL:CDM31107.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM31107.1};
RN [1] {ECO:0000313|EMBL:CDM31107.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM31107.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; HG792016; CDM31107.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QN81; -.
DR STRING; 1365484.W6QN81; -.
DR OMA; LDMGITF; -.
DR OrthoDB; 5481886at2759; -.
DR UniPathway; UPA00109; UER00180.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-UniRule.
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; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF29; PHOSPHOTRANSFERASE; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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|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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 49..287
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 299..490
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 526..619
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 68450 MW; B4812CE17DCD7F7A CRC64;
MASVNSKSSK KDEDEEHEIM HDDLIEDDEE ASSELNAVEQ ECLAHHQQLE EFLSPLFLDE
AVLYKLARRF STTYRNLALT SDQQFLPTPV TQLPTGRETG RYLAIDVGGS NLRVAFIELL
GEAVDSDVRP TDATERSRDT IRKAQRQRVK RTLERAWPIQ EHLKMDKAED LFSWIGDCIA
EVVAESLSSD ATKKDIPAEL DMGITFSFPI MQESLAEATL MPMGKGFAIS SNLNLGNILL
DGYEKHTRRP DDEDEPSTKR RKLFALPKLK IQAITNDTVA TLASLAYKVK SLPNSRVAMG
IIVGTGCNAT IPMKLSALHE SKAKSVNIME PSAVETVVNT EWTISGAAPP LKELNVTTKW
DIELDQACSR PGFQPFEYMT GGRYIGELIR LIIFDYLTTV AKLSKRSLPA NLIQEYALTT
TYISDVVAKA RSDNDLAKAL NKSLPPPECS DWRWDARAAG AFRKIARTVQ RRSAGLIAAA
VVGLLACARE IELKEDSNSS SPENPASPQI HGDTITESLS APDAAAASLN SAAVAASHAA
QEHVVPVLDP TPIDWQSGPE ELVVAYTGGI IQHYPQFKEM CQQYIDRLIM RTGPQRGGKS
VFLREASDGG VIGAGVLAGM VVRK
//