ID A0A319ACY3_ASPLB Unreviewed; 1243 AA.
AC A0A319ACY3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-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=BO96DRAFT_473570 {ECO:0000313|EMBL:PYH57175.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH57175.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH57175.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH57175.1,
RC ECO:0000313|Proteomes:UP000247441};
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 ---------------------------------------------------------------------------
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; KZ821347; PYH57175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ACY3; -.
DR OrthoDB; 2230730at2759; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000247441; 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; IPR018247; EF_Hand_1_Ca_BS.
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; SM00822; PKS_KR; 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; PS00018; EF_HAND_1; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 562..643
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 137616 MW; 6AF49A2A004E2EFE CRC64;
MASVAVSPIP SSLSSPNRLS ASSPATSIDE LDSEPSEETI HTINHLIQAR AKGRHGNEPI
VAYPSSGTEY TYYTPKQLDT LVEAASIHYS KIIPQRHSSD DPVQVVGLLG PSDFEYMITL
LAISRLGHTV LLLSTRIAED AYVSLIENTK AAFLITYPSF QAVGERVVSR TAIVQQPVLA
SENYDFPGAD TLSLPPAQLD GSVEAKHICW IIHSSGSTGH PKPIYQTHAG ALKNYANNFG
LRGFITLPLF HAHGISCLFR AIHSQKLIYL YNANLPLTAP HLLATLKDHQ EIEILYAVPY
ALKLLSESDE GLHMMARLEL VMFGGSSCPK PIGDKLVQNG VRLVSHYGTT ETGQLMTSFR
ERDDLDWDYV RPGPTLLPYL RWEEQMSGIY ELCVLEGWPS KVASNRPDNS YATKDLFEKH
PTKPNAWRYY ARLDDTLVLE NGEKANPLII EGVARNDPNV AEAIAFGANK PRLGLFLIPA
TSSRCQTDDQ LIEAVFPAIE RCNAELPAYA YISRDMIHVL PADASYRKTD KGTVIRAAFY
RDYQDQIDQI YEAEDASGDQ VLEGAELEAF LREQLLEVAP GIDPSTLGAT TDIFSLGVDS
LQSIRLRTTL LRTLDIGGHR LSQNFVFEYP SVQAMADELT RLRLGQAPKE QRPVEERMAD
LIEKYGNHFK PHTAVPREES GEHIVVTGAT GSLGAHIVAK LAQMDHVKTI YCLVRAESHE
AAFRRVRQSL RMRGLSSVLS PATERKVVAL PADLANPDRL GLDESLYNKL VQSVTAVIHC
AWSVNFNWAL ESFESSCIAG TRHLLDLCLD VHGPQPARFA FCSSVSTVAR TPGNWVPEAL
PDSLACAQGM GYAQSKLVTE HIVNRAAHQA GMTARVLRVG QIIADSVHGI WNATEAIPMM
FQTAETIHAL PQLDDILSWT PVDVVATSVI DLTMASGASE VVNLTNPMLN HWTRDLLPLL
RQAGLEFEEL PRREWLQRLR DSDQDPDVNP PIKLLEFFTS KYDHDRPSRV LLYDTKQAVA
GAPALREAGG LTPELVSRFI QHFRTHCWSS STGATTTLAP AREVIFLTGP CGCGKSTAAQ
ALAHRFEIPV IEGDNLHSPA ARAKMAKGIP LEDRDRWDWL AHIRGAVMDR LQQTTAPAVA
VTCSALRTVY RDELRQLSQL LDFPVTVTFL LLSVHDRETL KKRMVERLAK EEHYMRSTMV
DSQMDILEEP KLSEGDVIIV NAGQDKAQML QQVEETVRGL LKA
//