ID A0A1Y1VBZ0_9FUNG Unreviewed; 807 AA.
AC A0A1Y1VBZ0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN ORFNames=BCR36DRAFT_582435 {ECO:0000313|EMBL:ORX52494.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX52494.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX52494.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX52494.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001179};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000256|ARBA:ARBA00008375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX52494.1}.
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DR EMBL; MCFH01000015; ORX52494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VBZ0; -.
DR STRING; 1754191.A0A1Y1VBZ0; -.
DR EnsemblFungi; ORX52494; ORX52494; BCR36DRAFT_582435.
DR OrthoDB; 1326272at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd01678; PFL1; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR NCBIfam; TIGR01255; pyr_form_ly_1; 1.
DR PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 1.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 {ECO:0000256|ARBA:ARBA00023315};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818, ECO:0000256|PROSITE-
KW ProRule:PRU00493}; Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ORX52494.1}.
FT DOMAIN 84..677
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 684..807
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 782
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 807 AA; 89436 MW; 08F6ED0B115E8553 CRC64;
MESLTQVNNA IAKSVSVNTV AATKVAGVRI SKSTRAMHTI PMTTIGLKTS KKSSFPSIQT
KTYATQAQSI TNDAAAKSEI DVEGWIKKHY TPYEGDSSFL AGPTEKTKKL FAKAEEYLAK
ERANGGLYDV DPHTPSTITS HKPGYLDKDN EVIYGYQTDV PLKRAIKPFG GVNMVKNALA
AVNVPMDKEV EHIFSDYRKT HNTAVFDLYS KEMRSGRSNA IMTGLPDGYG RGRIIGDYRR
VALYGTDRLI AQKEKDRVEL QKNLMDEPTM KLIGEVADQI KALKQLTQMA KSYGIDISKP
AKNAREATQF VYFGYLGSIK EQDGAAMSLG RVDAFLDCFF ENDLKNGVIT EAEAQEIIDN
LILKLRFARH LRTPEYNDLF AGDPTWVTMS LGGMGSDGRT LVTKTSFRVL NTLYNLGPAP
EPNITVLWNK ALPKSFKDFA TQVSIDTSSI QYESDALMSA RFGNDYGIAC CVSAMRIGKD
MQFFGARCNL AKLMLYILNH GKDERTGKQV GPDFGPVPDG PIPFDWMWET YDKAMDWIAK
LYVNTMNVIH FSHDQYCYES LQMALHDTNV RRLMAFGVAG LSVVADSFSA IKYAKVTPIR
DQETGLTVDF KIEGDFPKFG NDDDRVDFFA KTVTDKLITK LRKTPTYRGA MHTLSILTIT
SNVVYGKKTG STPDGRKAGQ AFAPGCNPMH GREFSGAVAS LSSVAKVNYD SCMDGISNTF
SIVPNTIGKT LQERQGNLSG LLDGYFTKGA HHLNVNVLKR ETLEDAMAHP ENYPNLTIRV
SGYAVNFVKL TPAQQKEVIA RTFHEKM
//
