ID D8UHK4_VOLCA Unreviewed; 1486 AA.
AC D8UHK4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN ORFNames=VOLCADRAFT_107982 {ECO:0000313|EMBL:EFJ40790.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ40790.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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}.
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DR EMBL; GL378407; EFJ40790.1; -; Genomic_DNA.
DR RefSeq; XP_002958165.1; XM_002958119.1.
DR STRING; 3068.D8UHK4; -.
DR GeneID; 9623262; -.
DR KEGG; vcn:VOLCADRAFT_107982; -.
DR eggNOG; KOG2912; Eukaryota.
DR InParanoid; D8UHK4; -.
DR OrthoDB; 1326426at2759; -.
DR Proteomes; UP000001058; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:UniProt.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; IEA:UniProt.
DR CDD; cd01678; PFL1; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR010286; METTL16/RlmF.
DR InterPro; IPR004184; PFL_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF05971; Methyltransf_10; 2.
DR Pfam; PF02901; PFL-like; 2.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000001058};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 736..1355
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 1362..1486
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 349..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1461
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 1486 AA; 161521 MW; B007693AA7926E00 CRC64;
MEATMEAELL TAVAEYRAQL ASLEELLSAD PGNQEAKEVF RAGGVYEQLQ GALSYTLAAL
DEQQLQQQQQ LQEMADAQFA EGAAASRAAG ADEGPTTAIL HGNGDVDGVA AAVGGAAAVA
AAESDAVAEA LALAGAAAAS RPRGGAANNA RMHPANLYHR QEPDFAALAE KYKELRPYVS
TDAAGRAHLD TSSWAATRAL TACLLRHDFG VRWWLPEGQL VPPVPNRANY IHWINDLLHL
SAPPQPPQPP LSGCSGGGGG DGSDGACAVL RGLDIGCGAN FIYCLLGAVL YGWKMVGVDV
TQQIPVHPVQ VAVRCCRQLI EDNPQVAALL EIRDLSYLHP DLQAPDAAAL AGPVGPAGGG
RRRKRGGSAA GGPDGAAHAA ELQQQDYRED GGTGGDGTEA AEGGAVAMSG MDQEAGLPGD
AASPTGKQQG ILLPAFADDS ETFAFTMCNP PFFESMQEAA QNPNTAFGGT AAEMVCPGGE
LAFVLQMLVE SEELRDRVHW FSTMVGKKST LKALRRELHC RHVTALRTTE LAQGKTSRWA
VAWSWQVDPN KASQPLRRLD VPTAVTAAAV EPHGAAATST GPDAARLGRA PPVVAPSLAA
AGMPLLPRRH VSFTVQQTGF LNSRNFLQEV KRLLQAEGCG YQQQLEVDAV AWTVSWPLQV
GPFSAAAEGE ERTAKRHRED AAEGGRSWAS NIRAEMRVQS TYVGKEFGKR YHPAKHQVGV
LKQQMSNWTF MRTSGSRLFF APTRDHYELE PNLCACKRLD PRPRPAVDSG INVQKYVQEN
YKAYSGDSSF LAGPTERTKK LWSELEKLIC LELEKGVLDV DPSKPSTIAG FPPGYIDKDL
EQVVGLQTDK PLKRAIKPLG GINMVKAALE SYGYQPDAEV EQVYTSVRKT HNAGVFDAYT
DEMRAARKSG ILTGLPDGYG RGRIIGDYRH KTDLKHNLLG VMDEEKIRLR EEVNEQIRAL
MELKEMAQSY GFDISRPAQN SREAVQWLYF AYLGAVKEQD GAAMSLGRID AFLDTYFERD
LAAGTITEAE VQELVDHFVM KLRIVRQLRT PEYNALFAGD PTWVTCVLGG TDAAGKPMVT
KTSFRMLNTL YNLGPAPEPN LTVLWNENLP QPFKDFCSKV SLDTSSIQYE SDRLMSRLFG
SDYSIACCVS AMRVGKDMQY FGARANLPKL MLYVLNQGRD EVTGAQAGPK FASVRVKDAP
LDFEEVRAKL EDGMEWLASL YANTMNVIHY MHDKYDYERL QMALHDTYVR RLLAFGISGL
SVVTDSLSAI KYAKVTPVYD EKGIMVDFVV DGTFPKYGND DDRADEIAEW ITSTFSKKLS
SQHTYRNSIP TLSVLTITSN VVYGKKTGST PDGRKKGEPF APGANPLHGR DSHGALASLN
SVAKLPYTSC LDGISNTFSL IPQVLGKGGE PERAANLSSI LDGYFVTGGH HINVNVLNRA
MLMDAVEHPE KYPNLTIRVS GYAVHFARLT REQQLEVIAR TFHETM
//