ID A0A1V6T9S3_9EURO Unreviewed; 1236 AA.
AC A0A1V6T9S3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=PENSTE_c009G05903 {ECO:0000313|EMBL:OQE23122.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE23122.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE23122.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLKD01000009; OQE23122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6T9S3; -.
DR STRING; 303698.A0A1V6T9S3; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000191285; 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:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
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; 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:UP000191285};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 560..641
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1236 AA; 136122 MW; C4EC1F237E16D523 CRC64;
MAASVLTSPA ASALPITNTQ TSVSPEIALA SANHDIFTVD DLLQSRAAGE TAHEPIVAYP
SSGTEYIYYT PHQLNRLVES AAIYYSKTIP QRLTSTDPVQ VVGLLGPSDF EYLITLLAVS
RLGHTVLLLS TRIAEDAYVS LVEATKATFL VTYPSFESMG QNVSQRTNIT QVPVVSPTDA
NSPVVQAAHL PASNRHGPTE NKNITWVIHS SGSTGHPKPI YQTHSGALKN YANNFGLKGF
ITLPLFHAHG ISCLFRALHS QKLIYMYNAS LPLTATALLS TLNEHPEIEI LYAVPYALKL
LSESEDGLQR LARLELVMFG GSSCPKPIGD TLVQNGVRLV SHYGTTETGQ LMTSFRDRSD
LDWDYVRPGP SLLPYLRWEA QPGMPGIYEL CVTEGWPSKV ASNRPDNSYA TKDLFEKHPT
TPNAWRYYAR LDDTLVLENG EKANPLVIEG VARKNPNVAE AIAFGATKPR IGLFIIPSDK
SPFDNDEELL DAVFPDIDKC NAESPAYAYV SRDMIFVLPK DSEYRKTDKG TVIRSAFYKD
FAQQITDVYE SADATGDQVL EGEELIKFLR RELLEIAPAI EPSSLEPERD LFSLGIDSLQ
SIRLRTAILR TLDLGGQKLA QNFVFENPSL KAMADELTHL RLGNGPKTQI PVEERMQSLI
DKYSGGFKTH ISIPRVADGQ HIVLTGATGS LGAHIVAQLV HSDDVRKVYC LVRAKSVNSA
RRRVAQSLHT RKVSLALTPA AERKIVALPA DLTDSESLGL DEGTFSKLKK TATSVIHCAW
SVNFNWALES FEQSCIAATR NLLNFCLSVE APQPASFSFC SSVSTVARTP GNWVREELPE
SLSHAQGMGY AQSKLVTETI VNRASHQTGM TARVLRAGQI VADTSSGIWN STEAIPMILQ
TAKTIQALPK LDDILSWTPV DVMAASIIEL SLSSTAGEIL NVTNPTLNHW SNDLLPLLRE
SGLDFEELPK RAWLQTLQSS SQDPEVNPPI KLLDFFASKY DNDNPTRPLL YDTKKAQAAS
PSLANARGLN PEFTSQFIKY LDSQCWTKQP SPALPREVIF LIGPCGCGKT TAAQALSSRL
DIPTIEGDTL HSPIARQKMA RNIPLDDSDR WDWLAHIRGA VMDRLLTSDS PAVTVTCSAL
RTIYRDELRK LNQLFDFPVT VSFVMLSISD KAQLVERMNE RSVIEQHYMK SFMVESQLGL
LELPVDEDDV TLLDSSQSKD KMLDEVVEVV QNILKA
//
