ID R6SWA3_9CLOT Unreviewed; 671 AA.
AC R6SWA3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000313|EMBL:CDC61809.1};
GN ORFNames=BN660_01197 {ECO:0000313|EMBL:CDC61809.1};
OS Clostridium sp. CAG:448.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262808 {ECO:0000313|EMBL:CDC61809.1, ECO:0000313|Proteomes:UP000018074};
RN [1] {ECO:0000313|EMBL:CDC61809.1, ECO:0000313|Proteomes:UP000018074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:448 {ECO:0000313|Proteomes:UP000018074};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:CDC61809.1}.
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DR EMBL; CBFP010000174; CDC61809.1; -; Genomic_DNA.
DR AlphaFoldDB; R6SWA3; -.
DR STRING; 1262808.BN660_01197; -.
DR Proteomes; UP000018074; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:InterPro.
DR CDD; cd13944; lytB_ispH; 1.
DR CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR Gene3D; 3.40.50.11270; -; 1.
DR Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR003451; LytB/IspH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00216; ispH_lytB; 1.
DR PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF02401; LYTB; 1.
DR Pfam; PF00575; S1; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS50126; S1; 4.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018074}.
FT DOMAIN 321..390
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 408..477
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 494..562
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 579..648
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 644..671
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 671 AA; 73626 MW; 7BA4B05C9D487E9B CRC64;
MSVTVAKGAG FCFGVRRATE AVEAAIANRV QGEVIVTLGR LIHNNDYLSG LEATGVRTVS
EEDIPELCRF ADAAHPVRLF VRAHGMTAAI ERMLLRCAEE NPYFHFTDCT CPYVSKIHRI
VVEQTNADHP LFILGSANHP EVQGIVSRAK GQFWVFDSVN ALSALFDVEI KKQTTSKVPI
VVAQTTQKLE EWTKTKKFLK NHYTNAIIFD TICSVTDSRQ REAAILSQAS DFMIVIGGRD
SSNSAKLYSV CQSYCADTVW IENAAQLRIP VPFAHQRVGI TAGASTPRCI IEEVKETMSE
IMENDNFEAM LEKSLKTLNT GDTVTGYVTA ISAGEIQLDL GAKVTGRIEF DQITDDPSAK
LSDMFKIGDP VEAFVIRVSD LDGMATLSKK RVDSDKNWKN VEAAKESGEV LEGRVVEAVK
SGVIVSVGGV RVFVHESQTG APKDTDLHTL VGKTVRLKIT DIRDGKKARG SVRQVLRDER
RALEDAFWAN IEEGKYYTGV VKSMTSYGAF VDLGGVDGMV HASELSWKHI KSPAEILSIG
DEITVFVKSF DKEKKRISLG YKTEETNPWY IFTHTYAVGD VAPVKIVSMM PFGAFAEIIE
GVDGLIHISE IADHRIAKPA DVLEIGQVVD AKILDIDSEK QKVALSIRAL LEDAKAQEEA
AEAEAADESA E
//
