ID R7K883_9FIRM Unreviewed; 773 AA.
AC R7K883;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000313|EMBL:CDE71978.1};
GN ORFNames=BN810_00812 {ECO:0000313|EMBL:CDE71978.1};
OS Acidaminococcus sp. CAG:917.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=1262688 {ECO:0000313|EMBL:CDE71978.1, ECO:0000313|Proteomes:UP000018048};
RN [1] {ECO:0000313|EMBL:CDE71978.1, ECO:0000313|Proteomes:UP000018048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:917 {ECO:0000313|Proteomes:UP000018048};
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:CDE71978.1}.
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DR EMBL; CBJM010000004; CDE71978.1; -; Genomic_DNA.
DR AlphaFoldDB; R7K883; -.
DR STRING; 1262688.BN810_00812; -.
DR Proteomes; UP000018048; 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; 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; 3.
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; 2.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS50126; S1; 3.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW 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:UP000018048}.
FT DOMAIN 338..404
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 526..594
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 611..678
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 85579 MW; 38C6C2EA668698F9 CRC64;
MAERKIFLAK NAGFCMGVKS AVDKALELKG KCQVLGDIIH NETVIADLKS KGVNCVNDVL
SLDKNKTVLI RTHGAKKETI QHLSALGFKI EDCTCPFVKK IHEILNEKTS NGYFALIIGY
SGHDETEASL SYCNGKGVIL SDFSDIEKFL NTAAFDKLAV VAQTTFDNIK FENIVEKIKN
WSKGSVKTVE FFNTICYTTF DRQKEAVSLA TQCGAVAVVG SRSSANTTAL YRLAKQVNPN
TFFISGLNDL SFDINQFRSI AVLAGASTPT GLLLEVINAM SETQKTAQNA ENTTVTEKEA
TSQANKSPKK VKNEDEKLTM AQIVDNKELL NMTDYKPGKR VKCTVMSADD NGITISLGGK
KDGFISKEEA CYEGEYNPAD FKPGSEIEAV ILSNTHDSVL LSKKKIDAKR IEDEEAEKAL
KADVFTLEMT EVVKGGLRGR MGSYTVFVPA SHITTKYVSN LEDYKGKKLR LVVMPPKAKE
GQAENTEEAQ DKPQKKSKYI FASQRLVLER EKKEKEDAFW ESIHVHDIVE GKVKRFTEFG
AFVSVRGFDC LCHISEISWN KITDPSTVLK AGETYDFVVL KMDREANKIS LGYKQLQKKP
YEEAAEKYPV GTVIKGKVER IFPYGAFVSI DNGVDGLVHV SQIAHQYIKD ANEVLTVGQE
VEAKIIGFEG NRITLSIKAL LPEPEVREEG GAEEKKAKKT DGDKKEKKAK KTEKTDELRE
WHSDNSSATL GDLFKAFDLG IEEEAPAAPK KTRKKASTEE APAEETPSDD KKD
//
