ID A0A2G3E4H5_9FIRM Unreviewed; 480 AA.
AC A0A2G3E4H5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=[FeFe] hydrogenase H-cluster radical SAM maturase HydG {ECO:0000313|EMBL:PHU38101.1};
GN Name=hydG {ECO:0000313|EMBL:PHU38101.1};
GN ORFNames=CSX02_04290 {ECO:0000313|EMBL:PHU38101.1};
OS Agathobacter ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=1712665 {ECO:0000313|EMBL:PHU38101.1, ECO:0000313|Proteomes:UP000224563};
RN [1] {ECO:0000313|EMBL:PHU38101.1, ECO:0000313|Proteomes:UP000224563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK623 {ECO:0000313|EMBL:PHU38101.1,
RC ECO:0000313|Proteomes:UP000224563};
RA Sheridan P.O., Walker A.W., Duncan S.H., Scott K.P., Toole P.W.O., Luis P.,
RA Flint H.J.;
RT "Resolving the taxonomy of Roseburia spp., Eubacterium rectale and
RT Agathobacter spp. through phylogenomic analysis.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHU38101.1, ECO:0000313|Proteomes:UP000224563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK623 {ECO:0000313|EMBL:PHU38101.1,
RC ECO:0000313|Proteomes:UP000224563};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) 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:PHU38101.1}.
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DR EMBL; PDYG01000015; PHU38101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3E4H5; -.
DR Proteomes; UP000224563; 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 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; 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; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 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:UP000224563};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 283..390
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 480 AA; 54740 MW; 1D90F12B6E319EEF CRC64;
MYNVKSLKAE EFIDNQEILD TIEYAEANKY NFEFIEELLE KARPLKTAEG CVCRGLTHRE
ASVLLACDEP KYIEKMYQVA QEIKDAFYGN RIVLFAPLYL SNYCINGCVY CPYHAKNKHI
ARKKLTQEEV KAEVIALQDM GHKRLAIEAG EDPVNNPIEY ILECINTIYS IHHKNGDIRR
VNVNIAATTV ENYRKLKEAG IGTYILFQET YNKKSYEELH PTGPKHDYAY HTEAMDRAME
GGIDDVGLGV LFGLESYRYE FAGLLMHAEH LEAVHGVGPH TISVPRVKHA DDIDPEAFDN
SIPDEIFTKI AACIRIAVPY TGMIISTRES EEVRRKMLQV GISQVSGGSR TSVGGYTQEE
RPHDTEQFDV SDQRTLDEVV KWLMETGHIP SFCTACYRAG RTGDRFMSLC KTGQIINCCH
PNALMTLTEY LVDYASDETK EVGYKMIEEE LRKIPKENVR KTAAENIEAI KHSDRRDFRF
//