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Database: UniProt
Entry: A0A0C3REI6_9PORP
LinkDB: A0A0C3REI6_9PORP
Original site: A0A0C3REI6_9PORP 
ID   A0A0C3REI6_9PORP        Unreviewed;       499 AA.
AC   A0A0C3REI6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:KIO44921.1};
GN   Name=thiH {ECO:0000313|EMBL:KIO44921.1};
GN   ORFNames=BA92_07850 {ECO:0000313|EMBL:KIO44921.1};
OS   Sanguibacteroides justesenii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Sanguibacteroides.
OX   NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44921.1, ECO:0000313|Proteomes:UP000031980};
RN   [1] {ECO:0000313|EMBL:KIO44921.1, ECO:0000313|Proteomes:UP000031980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44921.1,
RC   ECO:0000313|Proteomes:UP000031980};
RA   Sydenham T.V., Hasman H., Justensen U.S.;
RT   "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT   genome.";
RL   Submitted (JUL-2014) 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:KIO44921.1}.
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DR   EMBL; JPIU01000038; KIO44921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3REI6; -.
DR   Proteomes; UP000031980; 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   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; SFLDG01060; BATS_domain_containing; 1.
DR   SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR   SMART; SM00876; BATS; 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:UP000031980};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          293..404
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   499 AA;  57268 MW;  D27249CF4DAA0E41 CRC64;
     MNVKDWTKNV IKQAEIDKYL VNGKDFIDEV EIFEELERQK NPDKQKVRDI IKKSLEIKIL
     TPAETATLLN VEDPELLLEM QEAALEVKRR VYDNRIVFFA PLYLSNLCVN SCVYCGFRAE
     NKEEKRHVLT MDEVREETAA VIDEGHKRMI AVYGEHPKNS ADYMADSIST IYATKRTTPT
     GNGFNNIRRV NVNAAPMEIA DLKKLWRAGI GTYQVFQETY HRGRYAELHP AHTIKGNYGW
     RLYAMHRAME AGIDDVAIGA LFGLYDWRFE VMGLLYHALD LERQFGIGPH TVSFPRMQPA
     PGSFISEHSP YLVTDEATKR LVTVIRLAIP YTGLIVTARE NPEFRRELIH MGCTQTDASS
     KIGIGAYSKK LRQEENSDKV QFMLGDQRSL DEVIRELAQD GMITSFCTAG YRCGRTGDKI
     MNLLEKGVEG KFCKLNAVLT FREYLNDYAS PETKAIGEQL IERELQEIEH TSFFTDKKLL
     PTFKSYYDRI AKGERDLYM
//
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