ID A0A089KY40_9BACL Unreviewed; 477 AA.
AC A0A089KY40;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:AIQ52735.1};
GN ORFNames=R70331_15245 {ECO:0000313|EMBL:AIQ52735.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ52735.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ52735.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ52735.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP009284; AIQ52735.1; -; Genomic_DNA.
DR RefSeq; WP_042176707.1; NZ_CP009284.1.
DR AlphaFoldDB; A0A089KY40; -.
DR STRING; 1536773.R70331_15245; -.
DR KEGG; paee:R70331_15245; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_0_0_9; -.
DR Proteomes; UP000029487; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE 4: Predicted;
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:UP000029487};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 87..302
FT /note="Elp3/MiaA/NifB-like radical SAM core"
FT /evidence="ECO:0000259|SMART:SM00729"
FT DOMAIN 276..388
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 477 AA; 53940 MW; D3C982009C97B239 CRC64;
MAHLRKDWEP ADFIDDAEIT ASLQEAGRTA GNRSVVQSIL DKARACKGLS HREAAVLLEV
RDEDILQDIY KSAKVIKEKI YGNRIVLFAP LYISNYCVNN CEYCGYKHSN QDFVRRKLNR
DELAGEVRVL QELGHKRLVI EAGEDPVHCD IDYVTDSIKT VYSVKVNNGS IRRVNINIAA
TTVEDYQKLR DAEIGTYILF QETYHRPTYA ALHKNGPKHD YDWHTTAMDR AQLGGIDDVG
VGVLYGLYDY KYDTVAMLMH AEHLEERFGV GPHTVSVPRL REAANVSLEM YPYLVKDEEF
KQLVAVLRLA VPYAGMILST REEPAFRDEV IQLGISQVSA GSSTGVGGYM EAKQGTAGAS
KEKPQFEVGD HRSPEEIIRG LCRDGYVPSY CTACYREGRT GDRFMRLAKS GQIHNVCQPN
SLLTFKEYLL DYADAETQAL GEEIIRKGLD DIPKEAARKI TRERLQRLEN GERDLRF
//
