ID A0A136IQB4_9PEZI Unreviewed; 1211 AA.
AC A0A136IQB4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=Micbo1qcDRAFT_125239 {ECO:0000313|EMBL:KXJ87112.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ87112.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-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}.
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DR EMBL; KQ964264; KXJ87112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IQB4; -.
DR STRING; 196109.A0A136IQB4; -.
DR InParanoid; A0A136IQB4; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000070501; 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 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.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 541..621
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1211 AA; 132838 MW; E69343C0F296479C CRC64;
MLTPPSSKSN DDDDSSIRTV DELVRRRART HPDRVIVSYP SEGTQYVDYT MQQLDVFAYR
VAKMYEQSLP MRRSSDEAPL TVAVLGPSNF DYLITMLALT KLGHTTLFLS TRISQDAVNS
LITTTDAICL LVDPRYTATA ESARAALPNL QLLQIVGRTS YDFPIEVHAD TRMDGHLDMS
VEANNLIYII HSSGSTGLPK PIHQPQKAAV ANYAVSMKMA ALITLPLYHN HGICNLFRAI
FSGKPIHLYN ADLPLTHNHL TNIMKTHRFE IFYGVPYALK LLSESELGLS LLRDLKIVMY
GGSAMPDALG DLLIAQGINL VGHYGATEVG QLMTSFREPG DDAWNYVRES PKLSPFLRWI
PRDQGLFECC VTEGWPAKVA SNQDDGSYLT KDLFEPHPTI PKAWKYIARR DDTINLETGE
MFNPVNTEGT IRSNKDVTEA IIFGAGRPVP GVLIVPAQCL EGKTDGEILE IVWPAVESAC
RDVEAYARIT KPMVKILPVG CDYPRTDKGS VIRQAFYKTY ADDIAEIYDR AERAGAEDLR
KLGSAELRRF VRQSLGQALG KAMTYDDHTD FFLLGLDSLQ ATQMRSDIIK TVDVGGHRLS
QTVVFDHPSV GQLSKYLFAL SDNQETEQDG AIEDEMRNLI NKYSRKPSTA AGAPAISVVL
TGATGSLGAH VLAKLVTDQT VDKVYCLVRA KSDDDAASRV RSSMLQRRVY HGLSLPQRRK
IFSLPSDLSR EDLGLSAEKL REVTASLGSV IHCAWSVNFN MRLSSFEQSN IAGVANLISL
CVSTRNVSGR TLPPASFNFC SSVSSVSRAT VDPVPESLPE LEWAQGMGYA QSKSVAEHLC
TQAAASGVTA RVLRVGQVVA DTKHGVWNST EAITMMLQAA TTIGALPRLR ETPSWLPVDT
TAESIAQISL SDAGSVFAHV ANPKTFDWTA DLLPALRQAG LQFEEVEPRE WVRRLRNSDP
DPVANPPIKL VDFFASKYDK DVFGPSKRYS TDVACSLAPA LADAPVLNTD FVIRFVSHFM
TGAWAKPSAL RGEAHPKTIV IVAGPCGSGK STLGSTLAHK LQSPFIEGDS LHTRSHIEKM
ASGQALSDAD RASWLQRVGR RAIESVVELG FDSAVVSCSA LRRSYRDALR AQVGDVARVI
FLDLQCGPEL LAKRISSRPG HYMPESLVKS QVLTYEPAAD SECDVLPVDA EASPGILLEE
AWRLLTQEHV I
//
