ID   VALC_STRHJ              Reviewed;         351 AA.
AC   Q3T6E2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=C(7)-cyclitol 7-kinase {ECO:0000303|PubMed:17335096};
DE            EC=2.7.1.214 {ECO:0000269|PubMed:17335096};
GN   Name=valC {ECO:0000303|PubMed:16151088};
OS   Streptomyces hygroscopicus subsp. jinggangensis (strain 5008).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1133850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5008 {ECO:0000312|EMBL:AAW88571.1};
RX   PubMed=16151088; DOI=10.1128/aem.71.9.5066-5076.2005;
RA   Yu Y., Bai L., Minagawa K., Jian X., Li L., Li J., Chen S., Cao E.,
RA   Mahmud T., Floss H.G., Zhou X., Deng Z.;
RT   "Gene cluster responsible for validamycin biosynthesis in Streptomyces
RT   hygroscopicus subsp. jinggangensis 5008.";
RL   Appl. Environ. Microbiol. 71:5066-5076(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5008 {ECO:0000312|EMBL:ABA41526.1};
RX   PubMed=16632251; DOI=10.1016/j.chembiol.2006.02.002;
RA   Bai L., Li L., Xu H., Minagawa K., Yu Y., Zhang Y., Zhou X., Floss H.G.,
RA   Mahmud T., Deng Z.;
RT   "Functional analysis of the validamycin biosynthetic gene cluster and
RT   engineered production of validoxylamine A.";
RL   Chem. Biol. 13:387-397(2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=5008;
RX   PubMed=17335096; DOI=10.1002/cbic.200600528;
RA   Minagawa K., Zhang Y., Ito T., Bai L., Deng Z., Mahmud T.;
RT   "ValC, a new type of C7-cyclitol kinase involved in the biosynthesis of the
RT   antifungal agent validamycin A.";
RL   ChemBioChem 8:632-641(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC       validamycin A. Catalyzes the phosphorylation of valienone and validone
CC       to their 7-phosphate derivatives. {ECO:0000269|PubMed:17335096}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + valienone = ADP + H(+) + valienone 7-phosphate;
CC         Xref=Rhea:RHEA:49420, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:111521, ChEBI:CHEBI:111522, ChEBI:CHEBI:456216;
CC         EC=2.7.1.214; Evidence={ECO:0000269|PubMed:17335096};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + validone = ADP + H(+) + validone 7-phosphate;
CC         Xref=Rhea:RHEA:49424, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:111523, ChEBI:CHEBI:111542, ChEBI:CHEBI:456216;
CC         EC=2.7.1.214; Evidence={ECO:0000269|PubMed:17335096};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=19 uM for valienone {ECO:0000269|PubMed:17335096};
CC         KM=26 uM for validone {ECO:0000269|PubMed:17335096};
CC         Note=kcat is 7.3 sec(-1) for validone as substrate. kcat is 3.5 sec(-
CC         1) for valienone as substrate. {ECO:0000269|PubMed:17335096};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to procduce
CC       validamycin A. {ECO:0000269|PubMed:17335096}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; AY753181; AAW88571.1; -; Genomic_DNA.
DR   EMBL; DQ164098; ABA41526.1; -; Genomic_DNA.
DR   RefSeq; WP_014668904.1; NC_017765.1.
DR   AlphaFoldDB; Q3T6E2; -.
DR   SMR; Q3T6E2; -.
DR   STRING; 1133850.SHJG_0278; -.
DR   OMA; GLMCECG; -.
DR   OrthoDB; 1130699at2; -.
DR   BioCyc; MetaCyc:MON-13773; -.
DR   BRENDA; 2.7.1.214; 14749.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Kinase; Transferase.
FT   CHAIN           1..351
FT                   /note="C(7)-cyclitol 7-kinase"
FT                   /id="PRO_0000443533"
SQ   SEQUENCE   351 AA;  35966 MW;  3B8585BFE2F06ECA CRC64;
     MTALTLAPCD LVVADLGGTT LRVGRITAGT SEVHDVKRVP TNGLGRYGAL APQELQDRVM
     EQLTREIAAH LTRPGQAPAQ AVAVSFAGPM TADGVVLAGP TLWGGPAAPL PVADVLTQRL
     GLPVVAANDV TAAAWRYAAA EPEPFCLTTV SSGIGNKVFR HGEIVIDQLG YGGEIGHWLV
     DHAEDAAPCE CGGRGHLGAI ASGRGALFAV RAAAAADASA FARSALAGPS GGVPEAITNE
     AFAAAARAGD TFARESLRRS LRPLASAVSL LFTAIGVRRY LFVGGFALAL GDTFLTLLGD
     ELVRVGCFGL DEYATRAMLA LGEDDDDHCL IGIGQLAAAR LGAPRAVEVT A