ID A0A081N5P2_9GAMM Unreviewed; 374 AA.
AC A0A081N5P2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:KEQ13765.1};
GN Name=thiH {ECO:0000313|EMBL:KEQ13765.1};
GN ORFNames=GZ77_15870 {ECO:0000313|EMBL:KEQ13765.1};
OS Endozoicomonas montiporae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ13765.1, ECO:0000313|Proteomes:UP000028006};
RN [1] {ECO:0000313|EMBL:KEQ13765.1, ECO:0000313|Proteomes:UP000028006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ13765.1,
RC ECO:0000313|Proteomes:UP000028006};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-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};
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:KEQ13765.1}.
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DR EMBL; JOKG01000003; KEQ13765.1; -; Genomic_DNA.
DR RefSeq; WP_034876916.1; NZ_JOKG01000003.1.
DR AlphaFoldDB; A0A081N5P2; -.
DR eggNOG; COG0502; Bacteria.
DR Proteomes; UP000028006; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR012726; ThiH.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR02351; thiH; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF1; 2-IMINOACETATE SYNTHASE; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 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:UP000028006};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 70..305
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 374 AA; 42672 MW; 383C68F7B0451DCF CRC64;
MSFLDTFNQL DWNEVKLSIT SKTASDVEQA LSASRLNHDQ FLALISPAAS PYLEQMAKKS
LQLTRQRFGN TVQLYIPLYL SNKCTNICTY CGFSLGNKIR RKTLSMDELD AEIRAIKAHG
FEHLLLVTGE APGTVGMDYF RKVLPKLRMH FSHISMEVQP LDQKDYEELM SLGLDAVLVY
QETYHRPTYN QVHLRGSKAD FDYRLETADR LGKAGIDKIG IGALIGLEDW RTDAAMVAAH
LDYLEKTYWR TRYSISFPRL RPCEGEMNPV SLISDRQLVQ LICAYRLFKP EAELSLSTRE
SARFRDNVLP LGITTMSAFS STQPGGYVND EFLEHTALEQ FAIDDNRRPE QVADAIRSKG
LEAVWKDWDN CYSH
//
