ID R7RPR3_9CLOT Unreviewed; 471 AA.
AC R7RPR3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=[FeFe]-hydrogenase maturation protein HydG {ECO:0000313|EMBL:CDF57366.1};
GN ORFNames=TCEL_01280 {ECO:0000313|EMBL:CDF57366.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF57366.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF57366.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF57366.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) 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:CDF57366.1}.
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DR EMBL; CAVN010000087; CDF57366.1; -; Genomic_DNA.
DR RefSeq; WP_018660441.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RPR3; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_0_0_9; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000014923; 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 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; 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; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 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:UP000014923};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 82..304
FT /note="Elp3/MiaA/NifB-like radical SAM core"
FT /evidence="ECO:0000259|SMART:SM00729"
FT DOMAIN 271..382
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 471 AA; 54229 MW; 125A5A3CBEE535D7 CRC64;
METVKQTFIN DNEIFKILDE AKKKAEDREY VLSILEKARE AKGLTPVEAA VLLNIEDREL
LDKMFKMAKE IKEKIYGRRI VLFAPLYVSN YCVNECEYCG YKHSNCSFKR KKLTMSELIE
EVKVLESLGH KRLALEAGED PQNCPIEYIL DCIRAIYSIK FDNGSIRRIN VNIAATSVEN
YRKLKEAEIG TYILFQETYH RETYEKMHKK GPKHNYDYHT TAMDRAMEGG IDDVGLGVLY
GLYDYKYETV AMLLHAQHLE EKFGVGPHTV SVPRLKKAEG VDLEKFPYLV SDEDFKKIVA
VLRLSLPYTG MILSTREEPK FRDEVIALGI SQISAGSCTG VGGYVEYYRG EHHDDEKPQF
EVGDHRSPLE IIKSLLRGGY IPSYCTACYR EGRTGDRFMR LAKTGQINNV CQPNALITLK
EFLLDYGDEE ARKLGEEVIK RELETIPNER AKEATIRMLE RIEKGERDLR F
//
