ID A0A069RK02_PEPLI Unreviewed; 500 AA.
AC A0A069RK02;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=2-iminoacetate synthase ThiH {ECO:0000313|EMBL:KDR96470.1};
DE EC=4.1.99.19 {ECO:0000313|EMBL:KDR96470.1};
GN Name=thiH {ECO:0000313|EMBL:KDR96470.1};
GN ORFNames=CLIT_2c00760 {ECO:0000313|EMBL:KDR96470.1};
OS Peptoclostridium litorale DSM 5388.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1121324 {ECO:0000313|EMBL:KDR96470.1, ECO:0000313|Proteomes:UP000027946};
RN [1] {ECO:0000313|EMBL:KDR96470.1, ECO:0000313|Proteomes:UP000027946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W6 {ECO:0000313|EMBL:KDR96470.1,
RC ECO:0000313|Proteomes:UP000027946};
RA Poehlein A., Jagirdar A., Khonsari B., Chibani C.M.,
RA Gutierrez Gutierrez D.A., Davydova E., Alghaithi H.S., Nair K.P.,
RA Dhamotharan K., Chandran L., G W., Daniel R.;
RT "Genome sequence of Clostridium litorale W6, DSM 5388.";
RL Submitted (MAR-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:KDR96470.1}.
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DR EMBL; JJMM01000002; KDR96470.1; -; Genomic_DNA.
DR RefSeq; WP_038260888.1; NZ_JJMM01000002.1.
DR AlphaFoldDB; A0A069RK02; -.
DR STRING; 1121324.CLIT_2c00760; -.
DR eggNOG; COG0502; Bacteria.
DR Proteomes; UP000027946; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:KDR96470.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027946};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 295..405
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 500 AA; 57233 MW; EE224BECFF745E01 CRC64;
MSKMNPKEWA SQVIVQEEID KYLVGGKDFI DEDEIFQKLS ENESPSPDRI RAILKKSLSI
KRLDPDETAA LLNVKDPDLI TEMEETALAV KRKVYDNRIV FFAPLYCSNL CVNSCLYCGF
RKDNSKEKRR TLSMDEIRRE TEHVIDEGHK RMIVVYGEHP LSDADYMAES IKAVYSVQRK
SKNGNGDGRI RRVNINAAPM RTSDLKKLAE IGIGTYQVFQ ETYHKDTYSR IHPEGPKSDY
RWRLYALHRA MDAGIDDLAI GALFGLYDWK FEVMGLLYHT MDLERQFGIG PHTISFPRLT
EAIGSDLSTN SKYIVSDEEF KRIVTVLRLS VPYTGLIVTA REKPGIKKEV IKLGCTQTDA
STNIDIGGYS ETVKEETADT QQFTLGETRS LDEVIGEVAD MGMISSFCTA GYRCGRTGDK
IMNLLTECVE GKFCKLNAIL TFKEYLEDYA SEKTRLVGEK LIQKEMEEVR QIPFFKQHNL
VEKLEEYYER ISNGERDLYL
//
