ID R5JFU2_9FIRM Unreviewed; 467 AA.
AC R5JFU2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:CCY47866.1};
GN ORFNames=BN738_00160 {ECO:0000313|EMBL:CCY47866.1};
OS Peptostreptococcus anaerobius CAG:621.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=1263100 {ECO:0000313|EMBL:CCY47866.1, ECO:0000313|Proteomes:UP000018261};
RN [1] {ECO:0000313|EMBL:CCY47866.1, ECO:0000313|Proteomes:UP000018261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:621 {ECO:0000313|Proteomes:UP000018261};
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:CCY47866.1}.
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DR EMBL; CAYH010000045; CCY47866.1; -; Genomic_DNA.
DR AlphaFoldDB; R5JFU2; -.
DR Proteomes; UP000018261; Unassembled WGS sequence.
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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
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; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 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:UP000018261};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 77..308
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 467 AA; 53693 MW; 1C7A472A796AE0F9 CRC64;
MNRMRFEENM KIDRDYVLSL IEGAKGTTDE EIDRILEKAK DKKGLDHSEI AALLEITRED
QAQKLFEIAG KIKRDVYGNR VVLFAPLYIS DYCVNNCVYC GYKCKNKFNR RRLTMDEIRK
EVEILEQMGH KRLALEAGED PVNCPIDYVL ESIKTIYDTY EKNGVIRRIN VNIAATTVEN
YRKLKEAQIG TYILFQESYD EEVYRKMHPN CIKGDYDYHT TAFDRAMEGG IDDVGAGVLF
GLADPKFEVL SLMLHNQHLE KKFGVGFHTI SVPRLRPAEG VNLETFPNLV DDEMFKKIVA
IIRLAVPYTG MILSTREDEE MRKFLLKYGI SQVSAGSCTG VGGYEEAANG RNIDQFEKAD
ERTPIEVITD LIDNDYIPSY CTACYRTGRT GEKFMSIAKS EKIHYMCKPN ALTTLMEYAV
DYGDEEFLKK AEKFVRDQAS TIDREDIREF TISNIQKLKD GQRDLYI
//