(data stored in ACNUC7421 zone)

HOGENOM: ECOL6_1_PE1012

ID   ECOL6_1_PE1012                       STANDARD;      PRT;   246 AA.
AC   ECOL6_1_PE1012; P0A9N5; P09374;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pyruvate formate-lyase 1-activating enzyme; EC=1.97.1
DE   4;AltName: Full=Formate-C-acetyltransferase-activating enzyme 1;AltName:
DE   Full=PFL-activating enzyme 1; (ECOL6_1.PE1012).
GN   Name=pflA; OrderedLocusNames=c1038;
OS   ESCHERICHIA COLI O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOL6_1.PE1012.
CC       Escherichia coli O6 (strain UPEC / O6:H1 / ATCC 700928 / CFT073)
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PFLA_ECOL6
CC   -!- FUNCTION: Activation of pyruvate formate-lyase 1 under anaerobic
CC       conditions by generation of an organic free radical, using S-
CC       adenosylmethionine and reduced flavodoxin as cosubstrates to
CC       produce 5'-deoxy-adenosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + dihydroflavodoxin +
CC       [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-
CC       methionine + flavodoxin semiquinone + [formate C-
CC       acetyltransferase]-glycin-2-yl radical.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79510.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000011458 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0A9N5; P09374; -.
DR   EMBL; AE014075; AAN79510.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_752967.2; NC_004431.1.
DR   ProteinModelPortal; P0A9N5; -.
DR   SMR; P0A9N5; 2-246.
DR   EnsemblBacteria; EBESCT00000044368; EBESCP00000042717; EBESCG00000043418.
DR   GeneID; 1038676; -.
DR   GenomeReviews; AE014075_GR; c1038.
DR   KEGG; ecc:c1038; -.
DR   GeneTree; EBGT00050000009897; -.
DR   OMA; LIGVPNK; -.
DR   ProtClustDB; PRK11145; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR012838; PFL_activating.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02493; PFLA; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR   HOGENOMDNA; ECOL6_1.PE1012; -.
KW   AAN79510.1000068575old_1320000031;
KW   Pyruvate formate-lyase 1-activating enzyme ;
KW   4Fe-4S; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Glucose metabolism; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   S-adenosyl-L-methionine.
SQ   SEQUENCE   246 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE VTVEDLMKEV
     VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI HTCLDTNGFV RRYDPVIDEL
     LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT LEFAKYLANK NVKVWIRYVV VPGWSDDDDS
     AHRLGEFTRD MGNVEKIELL PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY
     GHKVMF
//

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