ID A0A2P5HNV8_9PEZI Unreviewed; 1228 AA.
AC A0A2P5HNV8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-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=DHEL01_v209680 {ECO:0000313|EMBL:POS71927.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS71927.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS71927.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS71927.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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:POS71927.1}.
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DR EMBL; MAVT02001131; POS71927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5HNV8; -.
DR STRING; 158607.A0A2P5HNV8; -.
DR InParanoid; A0A2P5HNV8; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000094444; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR006001; Therm_gnt_kin.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01313; therm_gnt_kin; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 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; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000094444};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 564..643
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1228 AA; 135967 MW; B314F369BA76E5F3 CRC64;
MAPAAVVSTL WRPNEPMAAV TEQDAVGVER VEQVEDDSAL KTVDEVLRRR ARTDPNLPVV
SYPSSGIEYV DYTFQRLDVF AYRVGKQLQA VIPSRASSQE KRTVVAMLGP SNLEYLVTMM
ALFKLGHTVL FLSIRISVPA IKALIKSTGA TYLLANSRYL EPSLATKKQV PGLQVLDMPT
RTNFEFPIDV VGDTQLDGAL DPSVETTQIV YIIHSSGSTG LPKAIYQKQH AALSNFSGNM
NMKAFITLPL YHNHGICNLY RAVWSKKAIH LYNADLPLTC NYLIKILQAH RFEIFYGVPY
ALKLLAEADD GLSLLAQLKI VMYGGSACPD DLGDLLVQHG VNLVSHYGAT EVGQLMTSFR
QPGDKAWNYV REHDKLKPYL RWIPQGPNLF ECCVLPGWPA KTATNMDDGS YRTKDLFEPH
PTIPGAWKYI ARQDDTVVLV NGEKFNPVVT EGKIRSSKLV TEAVVFGAQQ PYLGVLVVPS
PAAAVNKSPA EILDLVWPIV QSAQQSDDAF AKISREMIVI LPHDVDYPRT DKGSLIRQMF
YRVFAKEIEL AYEISSSTNE NAREYTEAEV RGFLRTLVAK TLPQGTSFTD EADFFALGLD
SLQSIQMRAE ILRSVKTANK LTQNVVFDHP SIDKLAAYIS GSSTQTSIED EISALVEKYS
AFSTPRPKAG KFVAITGSTG SLGAHIVAQL VQDPSIDRIY CFVRAQDESS ATKRTTESLI
SRKLYHSLPL QLRRKVISLP ADLSKPDLGL PESTYREINS SLRTVIHAAW SVNFNIRLSS
FEKDNIAGVR HLIDLCQTGG ASFNFCSSVS TVARHPDNQG PVPESLPDAE WAQGMGYAQS
KCVAEAICAR AAQQAGIPVR VLRIGQIVAD TTHGVWNATE AVPLMLQSAL TIGALPRLTE
TPSWLPVDTV AKGVAEISLA DADRESKGAV FANVVNHRTF SWTEDLLPAL RNAGLDFEEV
EPKEWVRRLR ESNPDPVVNP PIKLVDFFAS KYDRDEFSPS KQYVTDTARS LSESLENAPL
LDKDFAKKFV DQFRKTSWKI SAARRDGEKT APAKRVIIVT GPCGSGKTTL ATALARSPIN
APFIEGDSLH SKTAIDRMHA GQPLSDEHRK PWLDRLVRRA HEELFELGYD TVVVSCSGLK
RAYRDQIRQI GADGRAEVVF LDLQCHPETL IARLQERKGH YMKAEMVQSQ LVDQEGIARD
EVDVFPIDAE DALGDILQWA TWALERIL
//
