ID K8EIZ2_9FIRM Unreviewed; 371 AA.
AC K8EIZ2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=2-iminoacetate synthase {ECO:0000313|EMBL:CCO08576.1};
DE EC=4.1.99.19 {ECO:0000313|EMBL:CCO08576.1};
GN Name=thiH {ECO:0000313|EMBL:CCO08576.1};
GN ORFNames=DESHY_40126 {ECO:0000313|EMBL:CCO08576.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08576.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO08576.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
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:CCO08576.1}.
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DR EMBL; CAOS01000011; CCO08576.1; -; Genomic_DNA.
DR AlphaFoldDB; K8EIZ2; -.
DR STRING; 1121428.DESHY_40126; -.
DR eggNOG; COG0502; Bacteria.
DR Proteomes; UP000009315; Unassembled WGS sequence.
DR GO; GO:0036355; F:2-iminoacetate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; 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; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 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 Lyase {ECO:0000313|EMBL:CCO08576.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 70..302
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 371 AA; 42225 MW; 2D4543C624614013 CRC64;
MGAVSFYRTY LSYSKLDFEA FFRRVTPDRV AGILHKQRLS PLDYLTLLSP AAEDFLEDMA
QRAYRLTVQH FGRTVLLYTP MYLANYCTNR CVYCGFAAHN QIKREKMTLA EVAAEARLIA
AGGLRHILIL TGESRQHTPV SYIRDCVQLL KKFFTSISIE IYPLAQEEYR ELIAAGVDGL
TIYQEVYNPE VYRQLHLAGP KRDYLWRLDA PERACRAGMR SVNVGALLGL HDWRSEAFFS
GLHANYLQSC FPAAEVSISP PRLRPHVGGM LPRVEVSDRN LVQYILAFRL FMPRGGITLS
TREPALLRDR LLPLGITRMS AGSCTAVGGR VKETVSEGQF AIADHRDVQS IVSMLYRQGY
QPVFKDWQWL E
//
