GenomeNet

Database: UniProt
Entry: R9KJZ4_9FIRM
LinkDB: R9KJZ4_9FIRM
Original site: R9KJZ4_9FIRM 
ID   R9KJZ4_9FIRM            Unreviewed;       472 AA.
AC   R9KJZ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=[FeFe] hydrogenase H-cluster radical SAM maturase HydG {ECO:0000313|EMBL:EOS43787.1};
GN   ORFNames=C809_03643 {ECO:0000313|EMBL:EOS43787.1};
OS   Lachnospiraceae bacterium MD335.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS43787.1, ECO:0000313|Proteomes:UP000014081};
RN   [1] {ECO:0000313|EMBL:EOS43787.1, ECO:0000313|Proteomes:UP000014081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COE1 {ECO:0000313|EMBL:EOS43787.1,
RC   ECO:0000313|Proteomes:UP000014081};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL   Submitted (APR-2013) 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:EOS43787.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASSW01000057; EOS43787.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9KJZ4; -.
DR   STRING; 1235793.C809_03643; -.
DR   PATRIC; fig|1235793.3.peg.3797; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_046249_0_0_9; -.
DR   OrthoDB; 9801120at2; -.
DR   Proteomes; UP000014081; 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:UP000014081};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          275..383
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
FT   REGION          341..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53854 MW;  0FECE85252041B8C CRC64;
     MYNVNSFRAE EFISDEEIRE TLEYADKNCD NMELVDAIIE KARQRKGLNH REASVLLACQ
     NEEKIKEIYA LANQIKNDFY GNRIVIFAPL YLSNYCVNGC LYCPYHLKNK HIARKKLTQE
     EIVREVTALQ DMGHKRLAIE AGEDPVNNPI EYILESIQTI YGIQHKNGAI RRVNVNIAAT
     TVENYRKLHD AGIGTYILFQ ETYHRESYER LHPTGPKHDY AYHTEAMDRA MAGGIDDVGL
     GVLFGLELYR YEFAGLLMHA EHLEAVHGVG PHTISVPRVK PADDINPDDF DNGISDDIFA
     KICALIRISV PYTGMIISTR ESQELRERVL PLGVSQISGA SRTSVGGYAQ PSQDNSTSEQ
     FDVSDKRSLD EVINWLIRLG FVPSFCTACY REGRTGDRFM TLCKNMQILN CCHPNALMTL
     KEYMEDYASE DTKRLGMELI ARELEKIPNP KVKERAAQNI REIEHGVRDF RF
//
DBGET integrated database retrieval system