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Database: UniProt
Entry: D8JYX4_HYPDA
LinkDB: D8JYX4_HYPDA
Original site: D8JYX4_HYPDA 
ID   D8JYX4_HYPDA            Unreviewed;       342 AA.
AC   D8JYX4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ADJ23576.1};
GN   OrderedLocusNames=Hden_1773 {ECO:0000313|EMBL:ADJ23576.1};
OS   Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS   TK 0415).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ23576.1, ECO:0000313|Proteomes:UP000002033};
RN   [1] {ECO:0000313|Proteomes:UP000002033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC   {ECO:0000313|Proteomes:UP000002033};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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};
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DR   EMBL; CP002083; ADJ23576.1; -; Genomic_DNA.
DR   RefSeq; WP_013215735.1; NC_014313.1.
DR   AlphaFoldDB; D8JYX4; -.
DR   STRING; 582899.Hden_1773; -.
DR   KEGG; hdn:Hden_1773; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_033172_0_0_5; -.
DR   OrthoDB; 9802027at2; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000002033; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR034422; HydE/PylB-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023858; RSAM_HmdB.
DR   PANTHER; PTHR43726; 3-METHYLORNITHINE SYNTHASE; 1.
DR   PANTHER; PTHR43726:SF1; BIOTIN SYNTHASE; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00330; HMD_cofactor_maturase_(HmdB-li; 1.
DR   SFLD; SFLDG01279; HMD_cofactor_maturase_(HmdB-li; 1.
DR   SMART; SM00729; Elp3; 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:UP000002033};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          50..267
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   342 AA;  37782 MW;  6FB646A83E507316 CRC64;
     MDFSELIAQV TRPDPPKELA LQLLQRSREP ALALQLFAAA SKIRDETMGK TLWWSAGISS
     MMPCRVEPLC TYCTYFTVKS FPLDELVASV KAIEDLGIRH LHLSGGTDLA GYDNELCEAV
     NAIRDVSSIE IEINLGPSLT RNGVRRLKQL GVASITSSLE TFNPEIFAKA KPGDSLDARK
     ALIEMCQDEG MPVRSMILVG LGESEADRID HLYWLLQFPR LYHLRFSRFM PYRGTSWEDH
     PRCSPWEVAR LVAVARLLMP HVDLGLAAGN SPDDIPLWYA AGGGNQVLGA SVSMRQGRVK
     AQPGETVIPV TDRVSLVSRM GHIEQFVRGL GRDIGSAAPQ LR
//
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