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Database: UniProt
Entry: A0A069AMK2
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ID   HYPDA_CLODI             Reviewed;         302 AA.
AC   A0A069AMK2;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 35.
DE   RecName: Full=Trans-4-hydroxy-L-proline dehydratase activating enzyme {ECO:0000303|PubMed:28183913};
DE            EC=1.97.1.- {ECO:0000305};
DE   AltName: Full=Glycyl-radical enzyme activating enzyme PflE {ECO:0000305|PubMed:28183913};
DE            Short=GRE activating enzyme {ECO:0000305|PubMed:28183913};
GN   Name=pflE {ECO:0000303|Ref.1};
GN   Synonyms=csdA {ECO:0000312|EMBL:SJP87434.1};
GN   ORFNames=BGU81_07855 {ECO:0000312|EMBL:PBG28509.1},
GN   BN1095_640055 {ECO:0000312|EMBL:CDT69048.1},
GN   BN1096_740113 {ECO:0000312|EMBL:CDS89457.1},
GN   BN1097_360076 {ECO:0000312|EMBL:CDS85121.1},
GN   C7R55_12960 {ECO:0000312|EMBL:PSJ82865.1},
GN   DDG63_17935 {ECO:0000312|EMBL:AWH82816.1},
GN   SAMEA3374989_01496 {ECO:0000312|EMBL:SJP87434.1};
OS   Clostridioides difficile (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Clostridioides.
OX   NCBI_TaxID=1496 {ECO:0000312|EMBL:CDS89457.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7032989 {ECO:0000312|EMBL:CDT69048.1}, and
RC   7032994 {ECO:0000312|EMBL:CDS85121.1};
RA   Monot M.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6636-R/ST48 {ECO:0000312|EMBL:PBG28509.1};
RA   Kociolek L.K., Ozer E.A.;
RT   "Genomic characterization of C. difficile isolates from children.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VRECD0007 {ECO:0000312|EMBL:SJP87434.1};
RG   Pathogen Informatics;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS-FS_0042_01 {ECO:0000312|EMBL:PSJ82865.1};
RA   Stone N., Sahl J., Wagner D.;
RT   "Clinical sequencing of C. difficile.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD161 {ECO:0000312|EMBL:AWH82816.1};
RA   Su H.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RC   STRAIN=70-100-2010;
RX   PubMed=28183913; DOI=10.1126/science.aai8386;
RA   Levin B.J., Huang Y.Y., Peck S.C., Wei Y., Martinez-Del Campo A.,
RA   Marks J.A., Franzosa E.A., Huttenhower C., Balskus E.P.;
RT   "A prominent glycyl radical enzyme in human gut microbiomes
RT   metabolizes trans-4-hydroxy-L-proline.";
RL   Science 355:1-28(2017).
CC   -!- FUNCTION: Catalyzes activation of the trans-4-hydroxy-L-proline
CC       dehydratase under anaerobic conditions by generation of an organic
CC       free radical on a glycine residue, via a homolytic cleavage of S-
CC       adenosyl-L-methionine (SAM). Is involved in the anaerobic
CC       degradation of 4-hydroxyproline. {ECO:0000269|PubMed:28183913}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q30W71};
CC       Note=Binds 2 [4Fe-4S] cluster. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:Q30W71};
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family. {ECO:0000305}.
DR   EMBL; LK932372; CDS85121.1; -; Genomic_DNA.
DR   EMBL; LK932529; CDS89457.1; -; Genomic_DNA.
DR   EMBL; LK933338; CDT69048.1; -; Genomic_DNA.
DR   EMBL; MPEQ01000010; PBG28509.1; -; Genomic_DNA.
DR   EMBL; FUNQ01000002; SJP87434.1; -; Genomic_DNA.
DR   EMBL; PXZF01000010; PSJ82865.1; -; Genomic_DNA.
DR   EMBL; CP029154; AWH82816.1; -; Genomic_DNA.
DR   RefSeq; WP_003432388.1; NZ_UIGU01000001.1.
DR   ProteinModelPortal; A0A069AMK2; -.
DR   EnsemblBacteria; CDS85121; CDS85121; BN1097_360076.
DR   EnsemblBacteria; CDS89457; CDS89457; BN1096_740113.
DR   EnsemblBacteria; CDT69048; CDT69048; BN1095_640055.
DR   PATRIC; fig|1496.1371.peg.375; -.
DR   eggNOG; ENOG4105F1A; Bacteria.
DR   eggNOG; COG1180; LUCA.
DR   Proteomes; UP000189432; Unassembled WGS sequence.
DR   Proteomes; UP000218405; Unassembled WGS sequence.
DR   Proteomes; UP000244883; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0043364; F:glycyl-radical enzyme activating activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040074; BssD/PflA/YjjW.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PTHR30352; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Repeat; S-adenosyl-L-methionine.
FT   CHAIN         1    302       Trans-4-hydroxy-L-proline dehydratase
FT                                activating enzyme.
FT                                /FTId=PRO_0000445029.
FT   DOMAIN       45     74       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       75    103       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   REGION       34     36       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   REGION      183    185       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        28     28       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        32     32       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        35     35       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q30W71}.
FT   METAL        57     57       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q30W71}.
FT   METAL        60     60       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q30W71}.
FT   METAL        93     93       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q30W71}.
FT   BINDING     133    133       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000250|UniProtKB:P0A9N4}.
FT   BINDING     257    257       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
SQ   SEQUENCE   302 AA;  34376 MW;  E8433F289198C84B CRC64;
     MNPLVINLQK CSIHDGPGIR STVFFKGCPL ECVWCHNPES QTYTKQVLYN EERCSKCEAC
     INICPHKAIY KGETKICLDQ DKCEFCETCL DYCVNNAREI VGQEYSVRDL VKEIEKDRIF
     YEESGGGVTL SGGEVMAQDM DFICGVINMC KSKGIHVAID TCGYAKSENY ERVAKCADLF
     LYDIKLIDED KHIKFTGKSN DLILKNVKIL SELGANINIR IPLIVGVNVD DENLEVKKMI
     EFLKPLNIQA VSLLPYHNIG KHKYDKIYKK YEGEELQRPS EEKLEEIKRL FEASNFNTKI
     GG
//
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