ID A0A0A2DZJ5_9PORP Unreviewed; 368 AA.
AC A0A0A2DZJ5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:KGN69649.1};
GN Name=thiH {ECO:0000313|EMBL:KGN69649.1};
GN ORFNames=HQ37_05520 {ECO:0000313|EMBL:KGN69649.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN69649.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN69649.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-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:KGN69649.1}.
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DR EMBL; JRAO01000019; KGN69649.1; -; Genomic_DNA.
DR RefSeq; WP_036881284.1; NZ_JRAO01000019.1.
DR AlphaFoldDB; A0A0A2DZJ5; -.
DR STRING; 1515613.HQ37_05520; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000030150; 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; 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 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:UP000030150};
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 368 AA; 42312 MW; 4E325F0D62150AF5 CRC64;
MAFYDELQRY DWDEVGCMIA STNEEQVQRA LAKERCTLDD FAALISPAAA PYLRQMATKA
ELLTTKRYGR TIQLYVPLYV SNYCSNHCVY CGFNCHNPIK RIKLDEKQIL EEIEVLKDWG
FRHLLLVSGE APHQAGVDYY AEVIRLLRPH FAQISLEVQP LQIEEYACLV DSGLSYVCVY
QETYNEQTYP SFHPRGAKAN FRYRLTTPER CAEAGVRKVG IGALLGLQDW RIDSFFTALH
LRYLEQHHWR SKYSISLPRL RPQVGGFEPE TPITDREMAQ LICAYRLFDP EVDISLSTRE
SAPFRDMAMH LGVTSMSAAS STEPGGYAHP QEELEQFTIN DDRSVQEICT AILAAGYETV
WKDWDTWM
//
