PFLB_HAEIN
ID PFLB_HAEIN Reviewed; 770 AA.
AC P43753;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Formate acetyltransferase;
DE EC=2.3.1.54;
DE AltName: Full=Pyruvate formate-lyase;
GN Name=pflB; Synonyms=pfl; OrderedLocusNames=HI_0180;
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=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.1.54;
CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Several mechanisms have been proposed based on complexes
CC formed with substrate analogs. After activation by the glycine radical,
CC the cysteine radical, Cys-420, can abstract hydrogen atoms from the
CC other active site cysteine, Cys-419, and from coenzyme A, and it can
CC also transfer hydrogen atoms to product radicals. The other active site
CC cysteine can attack the central carbonyl of pyruvate and covalently
CC bind the product acetyl group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC21849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC21849.1; ALT_INIT; Genomic_DNA.
DR PIR; F64052; F64052.
DR RefSeq; NP_438348.1; NC_000907.1.
DR RefSeq; WP_005653814.1; NC_000907.1.
DR AlphaFoldDB; P43753; -.
DR SMR; P43753; -.
DR STRING; 71421.HI_0180; -.
DR PRIDE; P43753; -.
DR EnsemblBacteria; AAC21849; AAC21849; HI_0180.
DR KEGG; hin:HI_0180; -.
DR PATRIC; fig|71421.8.peg.184; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_6; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR CDD; cd01678; PFL1; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR TIGRFAMs; TIGR01255; pyr_form_ly_1; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Organic radical; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..770
FT /note="Formate acetyltransferase"
FT /id="PRO_0000166688"
FT DOMAIN 5..635
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 642..770
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 419
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 420
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 745
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 770 AA; 86299 MW; 194AE21FDFB5CFBB CRC64;
MSELNEMQKL AWAGFAGGDW QENVNVRDFI QKNYTPYEGD DSFLAGPTEA TTKLWESVME
GIKIENRTHA PLDFDEHTPS TIISHAPGYI NKDLEKIVGL QTDEPLKRAI MPFGGIKMVE
GSCKVYGREL DPKVKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG
DYRRVALYGV DFLMKDKYAQ FSSLQKDLED GVNLEATIRL REEIAEQHRA LGQLKQMAAS
YGYDISNPAT NAQEAIQWMY FAYLAAIKSQ NGAAMSFGRT ATFIDVYIER DLKAGKITET
EAQELVDHLV MKLRMVRFLR TPEYDQLFSG DPMWATETIA GMGLDGRTLV TKNTFRILHT
LYNMGTSPEP NLTILWSEQL PENFKRFCAK VSIDTSSVQY ENDDLMRPDF NNDDYAIACC
VSPMIVGKQM QFFGARANLA KTLLYAINGG IDEKLGMQVG PKTAPITDEV LDFDTVMTRM
DSFMDWLAKQ YVTALNVIHY MHDKYSYEAA LMALHDRDVY RTMACGIAGL SVAADSLSAI
KYAKVKPVRG DIKDKDGNVV ATNVAIDFEI EGEYPQYGNN DNRVDDIACD LVERFMKKIQ
KLKTYRNAVP TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT
SVAKLPFAYA KDGISYTFSI VPNALGKDAE AQRRNLAGLM DGYFHHEATV EGGQHLNVNV
LNREMLLDAM ENPDKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTESM
