ID A0A1I2MEH5_9CLOT Unreviewed; 457 AA.
AC A0A1I2MEH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Iron-only hydrogenase maturation protein HydG {ECO:0000313|EMBL:SFF89894.1};
GN ORFNames=SAMN04487885_11465 {ECO:0000313|EMBL:SFF89894.1};
OS Clostridium cadaveris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1529 {ECO:0000313|EMBL:SFF89894.1, ECO:0000313|Proteomes:UP000182135};
RN [1] {ECO:0000313|EMBL:SFF89894.1, ECO:0000313|Proteomes:UP000182135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-G419 {ECO:0000313|EMBL:SFF89894.1,
RC ECO:0000313|Proteomes:UP000182135};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FOOE01000014; SFF89894.1; -; Genomic_DNA.
DR RefSeq; WP_074845768.1; NZ_FOOE01000014.1.
DR AlphaFoldDB; A0A1I2MEH5; -.
DR STRING; 1529.SAMN04487885_11465; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000182135; 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:UP000182135};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 261..368
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
FT REGION 327..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 52423 MW; D28B3CEA69D972E2 CRC64;
MFIDHEYIER ILDEAKSATK EDIQNILEKA KKRNGLSHED IAVLLQADDK NLKEMYKIAG
DIKNSIYGKR VVIFAPLYVS NYCVNNCVYC GYQRCNSFKR RKLTQEEVKD EVKILEKMGH
KRLALELGED PVNAPIDYVL ECLDTIYKTQ NSNGEIRRVN VNIAATTVEN YRKLKKDNIG
TYILFQETYH KPTYDKMHPK SIKGDYNYHL TAFDRAMEAG IDDVGGGVLF GLSDPKFEVL
ALMMHNEHLE EKFGVGFHTV SFPRLKKAKG MDLESFPNLL DDNMFKKIVA ITRIAIPFTG
IIMSTRESAE MRRELLKYGV SQVSAGSSTG VGGYKEREEG KEDEQFKTSD ERTPLEVLKS
LLDDGYIPSY CTACYRKGRT GERFMKLAKS GNIQYVCEPN AMMTLMEFAL DYGDKEILEK
SETLIKNEIN NIKRDDVREL VKNNLEKLKK GERDLYL
//
