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Multifunctional fusion protein [Includes: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (EC 1.17.7.4); Primosomal protein N' (EC 3.6.4.-) (ATP-dependent helicase PriA)]

 U5Q3Q0_9BACT            Unreviewed;       947 AA.
U5Q3Q0;
22-JAN-2014, integrated into UniProtKB/TrEMBL.
22-JAN-2014, sequence version 1.
25-OCT-2017, entry version 31.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|HAMAP-Rule:MF_00983};
Includes:
RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191};
Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191};
EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191};
Includes:
RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983};
EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983};
AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
Name=priA {ECO:0000256|HAMAP-Rule:MF_00983,
ECO:0000313|EMBL:AGY53192.1};
Synonyms=ispH {ECO:0000256|HAMAP-Rule:MF_00191};
ORFNames=BRDCF_p565 {ECO:0000313|EMBL:AGY53192.1};
Bacteroidales bacterium CF.
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales.
NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY53192.1, ECO:0000313|Proteomes:UP000017642};
[1] {ECO:0000313|EMBL:AGY53192.1, ECO:0000313|Proteomes:UP000017642}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CF {ECO:0000313|EMBL:AGY53192.1};
PubMed=24356833;
Tang S., Edwards E.A.;
"Complete Genome Sequence of Bacteroidales Strain CF from a
Chloroform-Dechlorinating Enrichment Culture.";
Genome Announc. 1:e01066-13(2013).
-!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-
butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl
diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in
the terminal step of the DOXP/MEP pathway for isoprenoid precursor
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00191}.
-!- FUNCTION: Involved in the restart of stalled replication forks.
Recognizes and binds the arrested nascent DNA chain at stalled
replication forks. It can open the DNA duplex, via its helicase
activity, and promote assembly of the primosome and loading of the
major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP-
Rule:MF_00983}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized
ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191}.
-!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized
ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-
methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-
sulfur] cluster + 2 H(+). {ECO:0000256|HAMAP-Rule:MF_00191}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00191};
Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
Rule:MF_00191};
-!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
methylbutenyl diphosphate: step 1/1. {ECO:0000256|HAMAP-
Rule:MF_00191}.
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000256|HAMAP-
Rule:MF_00191}.
-!- SUBUNIT: Component of the primosome. {ECO:0000256|HAMAP-
Rule:MF_00983}.
-!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP-
Rule:MF_00191}.
-!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
{ECO:0000256|HAMAP-Rule:MF_00983}.
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EMBL; CP006772; AGY53192.1; -; Genomic_DNA.
KEGG; bacc:BRDCF_p565; -.
KO; K04066; -.
UniPathway; UPA00056; UER00097.
UniPathway; UPA00059; UER00105.
Proteomes; UP000017642; Chromosome.
GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd13944; lytB_ispH; 1.
HAMAP; MF_00191; IspH; 1.
HAMAP; MF_00983; PriA; 1.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR003451; LytB/IspH.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005259; PriA.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF02401; LYTB; 1.
Pfam; PF04851; ResIII; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 3.
TIGRFAMs; TIGR00216; ispH_lytB; 1.
TIGRFAMs; TIGR00595; priA; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00191};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00983};
Complete proteome {ECO:0000313|Proteomes:UP000017642};
DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_00983};
Helicase {ECO:0000256|HAMAP-Rule:MF_00983};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00983};
Iron {ECO:0000256|HAMAP-Rule:MF_00191};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00191};
Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|HAMAP-
Rule:MF_00983}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00983};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191};
Primosome {ECO:0000256|HAMAP-Rule:MF_00983};
Reference proteome {ECO:0000313|Proteomes:UP000017642};
Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
DOMAIN 420 588 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 686 847 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
ZN_FING 651 663 C4-type. {ECO:0000256|HAMAP-
Rule:MF_00983}.
ZN_FING 678 694 C4-type. {ECO:0000256|HAMAP-
Rule:MF_00983}.
REGION 222 224 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00191}.
ACT_SITE 123 123 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00191}.
METAL 5 5 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00191}.
METAL 89 89 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00191}.
METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00191}.
BINDING 33 33 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00191}.
BINDING 67 67 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00191}.
BINDING 121 121 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00191}.
BINDING 159 159 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00191}.
BINDING 266 266 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00191}.
SEQUENCE 947 AA; 108149 MW; 2042C0279328FBEE CRC64;
MSGFCYGVVR AIEEAESFLD KNRKLYSLGS IVHNNTELDR LRKKGMEVVN HDDMKELKDS
VLFIRAHGEP PSSYETARKN NLRLIDCTCP VVLKLQKRIK EHYEEVRKIN GQLLIFGKKG
HAEVNGLVGQ TGGNAIVIEG AADLDSVDYS RPVVIFSQTT KDLDEYREIC RIIQQRIESA
GEPAGNFKSF NTICGQVSSR HPHLKEFAAK HSVIIFVSGK ESSNGKILFE SCKSVNPSSY
KIERIEEIKR EWFKEGDSVG VCGATSTPKW LLEEVAGYVK GEMFVNVILP LKFRDEVTYR
VPEQFNDTIE IGSVVRVNFA NKEYNAAVSA ISHSPGEYRG KIKEIINLSS EYKITENELK
LWDWMAKYYL CTQGEVYKAA YPSGISVTES KRKRRKPVRE VSESLPELSP AQKDAFLSIQ
EAFSAGKVAL LNGITGSGKT EIYIRLASEI IEKGENVLMM VPEIAMGRQL SSRLEKVFGE
SLLVYHSKQT RNERERVRRL LQDNKDRYLI LGTRSSLFLP FNKLGLIIVD EEHDQSYKQA
DPAPRYNGRD TALILSGFHS AYTLLGSATP SLETQYNTNN GKYALVRLNE RYYGTESPDI
EIVDTVRERK FGRMEGEFSR KILEAIKEKI DSNEQVMVFR NRRSYSPMVQ CMYCEEIPVC
PHCNVSLSYH KSRNELRCHY CNYHIRFNTI CTKCGNPGLR ERGIGTEKVE ERLREFFPSA
KIERFDFETT RSTVNEKKIL KEFSQGKTDI LVGTQMLSKG FDFEHLSLIC VLNAESMLTV
QDFRAEERAF QMLRQLAGRA GRKHSKGKIM IQTSRAEHPI YQHLLSNPEE QEGSIIAAQQ
LNEREEYGFP PYVRLIKITL KSTNKEKLHE AASLVSEKAP SWGAREWNGP FTPPLEKLMD
EHQLQFWIKL SRNNLLFEIK SVIASEIEEI EKRTRGSVKI IIDVDPN


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