ID A0A0D2E666_9EURO Unreviewed; 1253 AA.
AC A0A0D2E666;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=Z517_00913 {ECO:0000313|EMBL:KIW85521.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW85521.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW85521.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW85521.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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; KN846969; KIW85521.1; -; Genomic_DNA.
DR RefSeq; XP_013289329.1; XM_013433875.1.
DR AlphaFoldDB; A0A0D2E666; -.
DR STRING; 1442368.A0A0D2E666; -.
DR GeneID; 25300403; -.
DR VEuPathDB; FungiDB:Z517_00913; -.
DR HOGENOM; CLU_002220_2_1_1; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000053029; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR006001; Therm_gnt_kin.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 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:UP000053029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 561..642
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 137973 MW; 831D256521FCCE7D CRC64;
MASVDMRSPL PVSKVSPVAS PSLQPPTPPL SPPLPSPRTI TELLSLRARD FPDEPIFGYP
SDALDYLEYT YSDLVRISSQ AARRYAECLP SRTDSHQETR VIALLGPSDL DYFFTLLALS
RLGFTVLFLS TRISQAAYLS LLDVTKCRHI VVGSSFRKTA NALAAARDGL EVIDILTQAQ
YMTNTQLDDA ALQQQHFDLD QESSKVAWII HSSGSTGLPK PIYQTHKAAL KNYENSLRMR
GFVTLPLFHA FGLSNVFRGI TAVKKIYIYN ANLPLTSQHL LKILTDHEFE IFLAVPYALK
LLSETHDGIN ALAALKVVMF GGSACPDALG DLLTEGGVNL ISHYGTTETG QLMTSFRPAD
DKAWNYVREH DQLKPYLRME PQGGNLYELC VLDGWPSKVA TNRDDGSYAT KDLFEPHPSI
PGAWKYCGRL DDTLVLVNGE KAIPLAMEQA LRQNKLVREA VMFGTGKSQL GMMVIASEQG
AGMSAGDLLE SIWPTIMAEN KALPAYAQLA KEMITVLPAG TAYPCTDKGS LIRQAFYRAF
HNEIEEVYHQ AESRTAGTLV LSELELREFI RGHLLDLCPQ DESTCLTDDT DLFSLGVDSL
HSTRLRAKIL QEVQLNGNSL PQNIVFEYPT IAKLAAAILN IRDRKSGETQ DVVKEMERLV
EKYSEFPQHI PVPSKSTGRC IVVTGATGSL GAHLVAQLVR RQDISEVCCL VRASSRSSAR
RRVIESMQRR ALYHTLPLDL RRKISCYPSD FSKTDLGLGD SVYASISAKI TSLVHCAWSV
NFNKNLSSFE ADCIAGTRHL MLLCLSAQQP TPASFNFCSS VSTVTNTPGD AVAEALPQSF
KCAQGMGYAQ SKLVTEHLVT RAASQTGMEA RVLRVGQIIA DTAHGIWNDT EAIPLMLQAA
TTIGALPTLD EHPRWLPVDS VARVVMDISL SSTTHAVFNI VNPRTFHWTN DLLPALHNAG
LSFAQVNQRE WIRRLRASNP DPEQNPTIKL VEFFSSKYDN DLTKRKNFKY VTSTAEQISP
ELGMVPALST DLVKKFVGHF LKTNWTATAP TAGSRQQQST RLIVLSGPPG VNKSTLAIEL
AESLSCPVID GDAVHDAIAK VKMSSGIHLS SLDRQIWLAR IKLEVLERVR ADQIVHGDQP
KSSGRSGKDV ILTCSALSRS DRNTLRNILS RSNDETEAEY INTVFVVLQA TEDEILRRVG
DGQRNTMKLD MVAPRLDTTG HADVDEPDIF PVDAEQEMEA IIQEALGGLA VLT
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