ID B0VHH9_CLOAI Unreviewed; 469 AA.
AC B0VHH9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Fe-hydrogenase assembly protein,S-adenosylmethionine radical protein {ECO:0000313|EMBL:CAO80794.1};
GN Name=hydG {ECO:0000313|EMBL:CAO80794.1};
GN OrderedLocusNames=CLOAM0921 {ECO:0000313|EMBL:CAO80794.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO80794.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO80794.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CU466930; CAO80794.1; -; Genomic_DNA.
DR RefSeq; WP_015424652.1; NC_020449.1.
DR AlphaFoldDB; B0VHH9; -.
DR STRING; 459349.CLOAM0921; -.
DR KEGG; caci:CLOAM0921; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_0_0_0; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000002019; Chromosome.
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.
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:UP000002019};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 77..309
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 469 AA; 53401 MW; 463AA4480A8CFD40 CRC64;
MKINTEGLKS FIPTAEIEEH LNKNRFADAI RIRDIVDKSL DKQRLNPDET AALINVTDPE
LKNLILEGAH TLKERIYGNR IVLFAPLYVG NECINDCVYC GFRISNKECQ RATLSKEELI
AETEALEDKG HKRLIMVYGE HPKYSPEFIA ETVQTVYNVK HNKGEIRRVN INAAPLDIEG
FRTVKSVGIG TYQIFQETYQ EETYQNLHPR GPKSNFLWRL YGLDRAMQAG IDDLGIGALM
GLYNWRFEVM GLLYHTIHLE ERFGVGPHTI SFPRIEPAIG TDFTKNPPYK VSDEDFKLLI
ASIRLSVPYT GMILTAREPI AVRDEVLRYG ISQIDAGSSI GVGDYAHKDE ESKRKSQFVL
GDTRTLDDVI YELAHSGYIP SFCTSCYRAG RTGEHFMEFA IPGFVKRFCT PNALLTFAEY
LYDYASERTK KIGLELIDKE VAKIDDPNMQ SSVQENLAKM KEGIRDLHY
//
