ID A0A2I2GHI9_9EURO Unreviewed; 1234 AA.
AC A0A2I2GHI9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=gluconokinase {ECO:0000256|ARBA:ARBA00012054};
DE EC=2.7.1.12 {ECO:0000256|ARBA:ARBA00012054};
DE AltName: Full=Gluconate kinase {ECO:0000256|ARBA:ARBA00029835};
GN ORFNames=P170DRAFT_402431 {ECO:0000313|EMBL:PLB52351.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB52351.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB52351.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB52351.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12; Evidence={ECO:0000256|ARBA:ARBA00001329};
CC -!- PATHWAY: Carbohydrate acid metabolism. {ECO:0000256|ARBA:ARBA00004761}.
CC -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC {ECO:0000256|ARBA:ARBA00008420}.
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:PLB52351.1}.
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DR EMBL; MSFO01000002; PLB52351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GHI9; -.
DR STRING; 1392250.A0A2I2GHI9; -.
DR VEuPathDB; FungiDB:P170DRAFT_402431; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02021; GntK; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006001; Therm_gnt_kin.
DR NCBIfam; TIGR01313; therm_gnt_kin; 1.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 555..636
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1234 AA; 137304 MW; 9332565A5CC33B9F CRC64;
MASVQIQPVT PSPVPALLTP SRVVPVVSSE REEQVIYTID GLLRARAAGD KADEPIVAYP
AEGTEYAYYT PRQLHTFVEA AAVHYSKVIP QRRSSQDAVQ VVGLLGPSDF EYLITLLAIS
RLGHTVLLLS TRIAEDAYVS LVESTKTTFL VTHASFQKMG ENVAQRTGVI RQSVLSREDY
ELPVAVDLPA AQLDAQTEAK HVCWVIHSSG STGHPKPIYQ THSGALRNYA NNFGLRGYIT
LPLFHAHGIS CLFRAVHSQK LIYMYNANLP LTAPSLLATL HDHPEIEVLY AVPYALKLLS
ETEEGLKKMA RLDLVMFGGS SCPKPIGDKL VQNGVRLVSH YGTTETGQLM TSFRDRSDLD
WDYVRPGPTL LPYLRWEEQM PGIYELSVLE GWPSKVASNR PNGSYATKDL FEKHPTKENA
WRYYARLDDT LVLENGEKAN PLVIEGVARN NPNVAEAIAF GANKPRLGLF LVHAENSSKT
DGELVDSAFP AIEQCNAESP AYAYISRDMI RVLPADAEYR KTDKGTVIRS AFYRDYQEQI
DLIYDSEDAQ GDKVLEGDEL LDFLREQLLQ IAPSIEPSSL NNTTDIFGLG VDSLQSIRLR
SVILKTLDLK GQKISQNFVF ENPSVQAMAD ELTRLFLGDS KEEVPVEDRM QNLIRKYTEQ
IPAHISLSRD YDGEHVVVTG ATGSLGAHVV AQLARSDNVR RIYCLVRAKT KHAAYRRVRQ
SLRDRAVLED LTSDVQRKIV ALPSDLSDGK LGLDFDTYHE LMECATAVIH CAWSVNFSWS
LESFEQSCIA GTRNLLGFCL NVRAPQPARF SFCSSVSTVA RTPGGWAPEA LPESLSYAQN
MGYAQSKLVT EHIVNRVAQQ TGMSARVLRV GQIIGDTVHG IWNDSEAIPM ILQTAKTIGA
LPQLDDVLSW TPVDTIASSV IDLTLAEDAG EVMNVTNPIL KHWTYDLLPL LKQAGLDFEV
VDRQEWLRRL LNSNRDPAAN PPIKLLPFFA NKYGHNHSKS FLFYSTNLAQ AAAPALRQAG
GLTQELVTRF ARYFQNECWN QTASSPPISA QRTSEVIFLI GPCGCGKTTA AHAITERLGL
PVIEGDDMHS PAARKKMSNK IPLTDEDRWE WLAHIRGAVM DRLQQHRDIP GLVVTCSALR
TVYRDRLRRL SELFDFPVGV TFLLLDIHDK EKLEDRLVAR SEGEGHYMAA SMVDSQLELL
EEPDMSEGDI IRVNSSQGKW DMLRDVEARA NSIL
//
