ID A0A0B7MMX7_9FIRM Unreviewed; 543 AA.
AC A0A0B7MMX7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hydroxymethylbutenyl pyrophosphate reductase {ECO:0000313|EMBL:CEO89067.1};
GN ORFNames=SSCH_360004 {ECO:0000313|EMBL:CEO89067.1};
OS Syntrophaceticus schinkii.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Syntrophaceticus.
OX NCBI_TaxID=499207 {ECO:0000313|EMBL:CEO89067.1, ECO:0000313|Proteomes:UP000046155};
RN [1] {ECO:0000313|Proteomes:UP000046155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sp3 {ECO:0000313|Proteomes:UP000046155};
RA Manzoor Shahid, Zubair Saima;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767}.
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DR EMBL; CDRZ01000232; CEO89067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MMX7; -.
DR Proteomes; UP000046155; 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; 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; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 1.
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 PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 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 3: Inferred from homology;
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:UP000046155}.
FT DOMAIN 170..239
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 257..323
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 344..412
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 429..498
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 67..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 59847 MW; 62C7EDEC54931EBD CRC64;
MLTHANWWIF VEKKVPTHHI EDAGELTPEM LRGASVVGVT AGASTPDWII EEVIERMTMF
DEEMEKVEEG AVEAAADATP EAVAEDAPVA NEELSESREP TELSGQSEEA ETAEPSELSG
QSEESEESEP SEPSELSGES EESEESELSE PDQEAMMNLD LGTPRQIKQG DLISGAVVQV
RDDEVLIDIG GKSEGVIPRR ELALKDADDV LENINVGDVL DVYVLRVDND EGHLILSKKR
ADRAKALDFL EKAMEEKTEL AGEVVRVVKG GLLVDVHGVR GFVPASLIER GYAGDLEKYL
EKILRLRVIE FDRSKAKVVL SQKAILQEEF LKAQKELWET IEAGEIRKGT VRHLTNFGAF
VDLGGVDGLL HISELSWGRV KHPSDVVQEG DEIEVYVLSV DKENKRISLS LKQVQGNPWD
KVDENYNVGE IVTGKVMRTV SFGAFVQLEP GVEGLVHISR MADYHVVKPE DVVNAGDEIK
VKILDINKQD QRISLSIKDA QENKTEDKGN NQEGSEQSHT SSSSVGVNLG EVFGDLLTRA
EHK
//
