Y520_HAEIN
ID Y520_HAEIN Reviewed; 262 AA.
AC P44743;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative glycyl-radical enzyme activating enzyme HI_0520 {ECO:0000305};
DE Short=GRE activating enzyme HI_0520 {ECO:0000305};
DE EC=1.97.1.- {ECO:0000250|UniProtKB:P0A9N4};
GN OrderedLocusNames=HI_0520;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000250|UniProtKB:P0A9N4};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0A9N4};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P0A9N4};
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22178.1; -; Genomic_DNA.
DR PIR; B64154; B64154.
DR RefSeq; NP_438678.1; NC_000907.1.
DR RefSeq; WP_005694124.1; NC_000907.1.
DR AlphaFoldDB; P44743; -.
DR SMR; P44743; -.
DR STRING; 71421.HI_0520; -.
DR PRIDE; P44743; -.
DR EnsemblBacteria; AAC22178; AAC22178; HI_0520.
DR KEGG; hin:HI_0520; -.
DR PATRIC; fig|71421.8.peg.539; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_3_0_6; -.
DR OMA; CHNPHTI; -.
DR PhylomeDB; P44743; -.
DR BioCyc; HINF71421:G1GJ1-533-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352; PTHR30352; 2.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..262
FT /note="Putative glycyl-radical enzyme activating enzyme
FT HI_0520"
FT /id="PRO_0000200543"
FT DOMAIN 20..262
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 40..42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 130..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ SEQUENCE 262 AA; 29496 MW; D76E061F201AFC3F CRC64;
MTALSEIFVP LHRIIPFSNV EGQGNRSSIF LQGCKLNCLY CHNPETIPRY TESAKLVSLQ
YLYEQVMEAV PFIRGVTVSG GEPTIHHKKL VPLFKALRSQ GLTCYLDSSG FFEFDRVCSL
IDVTDKFLFD LKGEGIGLQT LCFDRKNQAG IVPQQVIPER LHIKNDKLER NLQNLAALLP
LNKVEEVRLV FLKHFFDAEH LVGKVAQLLR NYPDVALKII RVHSKGVRDE AGLSAYIPSV
EETNALSAYA RQCGINKILT IL
