ID G7UUC5_PSEUP Unreviewed; 710 AA.
AC G7UUC5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000256|HAMAP-Rule:MF_02205};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_02205};
GN Name=dinG {ECO:0000256|HAMAP-Rule:MF_02205,
GN ECO:0000313|EMBL:AER55014.1};
GN OrderedLocusNames=DSC_01805 {ECO:0000313|EMBL:AER55014.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55014.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER55014.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER55014.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase.
CC {ECO:0000256|HAMAP-Rule:MF_02205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02205};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02205};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02205};
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1 sub-
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02205}.
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DR EMBL; CP003093; AER55014.1; -; Genomic_DNA.
DR RefSeq; WP_014159192.1; NC_016147.2.
DR AlphaFoldDB; G7UUC5; -.
DR STRING; 1045855.DSC_01805; -.
DR KEGG; psd:DSC_01805; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_4_1_6; -.
DR OMA; PRRAQNY; -.
DR OrthoDB; 9805194at2; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_02205; DinG_proteobact; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR039000; DinG_proteobact.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472:SF59; ATP-DEPENDENT DNA HELICASE DING; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02205};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02205}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_02205, ECO:0000313|EMBL:AER55014.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02205};
KW Iron {ECO:0000256|HAMAP-Rule:MF_02205};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02205};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02205}; Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT DOMAIN 34..323
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
SQ SEQUENCE 710 AA; 76462 MW; F6CEC2869A1A5898 CRC64;
MSDRTGPAAD HDTASTGRSL DEALKTRIRD AYAALRDATP GFTTRRAQSQ MIGVVARALG
TSGGVGVIEA PTGVGKSLGY LTAGVPIALA AGKKLVISTG TVALQAQLVE RDIPAFLKAT
GIQASVALAK GRTRYLCTRN VAELQGEVTG QESMFGDEGA LYDRPLTPAD TALVNRLAAL
FTDSQWNGDL DASPEPVSPT LRARITTNAA GCAGRRCSYA SQCPVLKARN HVREAQIVVT
NHALLLSTLS LGEGENGQPL IAPPDQMLLV LDEGHHVAGV AIGQGAARLP MDDMSRRTSR
LQTLIAATYR MVDKDTISQL HPNEAIELAA NVSRQLKAFR EALDAAWTPD PSERQPQWRA
PNGRLPPDWS PAIEALADDT RNLLNWVSAA APLVGKSKHD DATKERVQRN LGIALEMIQS
QHALWAGWKR QDPDGVPPMA RWMTRERDGE LVCHCSPVSA AQVLGQLLWK QVDSVVMTSA
TLTGGNGFTA LAIDTGLPEH AEAVSLSSPF DLARQAQLVV PRFPAAPDDR EGHPQEVARY
LVRELDWGKG SMALFTSRWK MEKVADLLPV TQRNRVLVQG EGNKSQIIAE HLRRIGAGEG
SVLFGLNSFG EGLDLPGEAC TTVVITQVPF AVPTDPQTAT LSEWLEGRGH NAFNLIAIPH
ALRMLTQFAG RLIRTSTDSG RVIILDSRLL SRRYGRQIID ALPPFARVIG
//