UniProt: A0A248YVS1

Database: UniProt
Entry: A0A248YVS1_9ACTN

LinkDB:  A0A248YVS1_9ACTN 
Original site:  A0A248YVS1_9ACTN

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (3)   
All databases (15)   

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ID   A0A248YVS1_9ACTN        Unreviewed;       747 AA.
AC   A0A248YVS1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Formate acetyltransferase {ECO:0000256|RuleBase:RU368075};
DE            EC=2.3.1.54 {ECO:0000256|RuleBase:RU368075};
DE   AltName: Full=Pyruvate formate-lyase {ECO:0000256|RuleBase:RU368075};
GN   Name=pflB {ECO:0000313|EMBL:ASW57748.1};
GN   ORFNames=CIK06_15695 {ECO:0000313|EMBL:ASW57748.1};
OS   Plantactinospora sp. KBS50.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Plantactinospora.
OX   NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW57748.1, ECO:0000313|Proteomes:UP000216795};
RN   [1] {ECO:0000313|EMBL:ASW57748.1, ECO:0000313|Proteomes:UP000216795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS50 {ECO:0000313|EMBL:ASW57748.1,
RC   ECO:0000313|Proteomes:UP000216795};
RA   Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT   "Genome sequencing and analysis of secondary metabolite biosynthetic
RT   capabilities of Plantactinospora sp. KBS50.";
RL   Submitted (AUG-2017) 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         ECO:0000256|RuleBase:RU368075};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC       step 1/1. {ECO:0000256|RuleBase:RU368075}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU368075}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000256|ARBA:ARBA00008375,
CC       ECO:0000256|RuleBase:RU368075}.
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DR   EMBL; CP022961; ASW57748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248YVS1; -.
DR   KEGG; plk:CIK06_15695; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000216795; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
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   ECO:0000256|RuleBase:RU368075};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU368075};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW   Glucose metabolism {ECO:0000256|RuleBase:RU368075};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216795};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT   DOMAIN          1..617
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          624..747
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   ACT_SITE        411
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        412
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   MOD_RES         722
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   747 AA;  82835 MW;  E1AAB644145549AE CRC64;
     MRNPTERGAW RGFTGQGWRA RINVAAFVRD NVTPYRGGPD FLTGPTPRTT ALWDGLRAMF
     VEERRRGIHD VDTRTPAGIT AHRPGYLDRD RELIVGLQTD APLRRAIMPA GGLRMVEAGL
     AAYGYELDPT VRQIFGTYRK THNEGVFDAY PADVRAARRS HIITGLPDAY GRGRIIGDYR
     RVALYGVDRL VFDRRALKEA LDERHSTVDV IRDREELAEQ IRALDELKRM AAGYGYDIGR
     PAETGREAIQ WLYFGYLGAA KEQNGAAMSL GRTASFLDCY LQRDLAEGTL TETGAQELID
     DLVIKLRIIR FLRTPEYDEF FSGDPTWVTE ALGGLGADGR PLVTRTTYRY LQTLYNLGPA
     PEPNLTVLWS PALPTEFKRF CARVSLDTSA IQYENDDLLR PRYGDDAAIA CCVSAMRVGR
     DMQFFGARAN LAKALLYAIN GGRDELTGAQ VAPAGPPVDG EYLDYAQVTA ALDRTLDWLA
     ETYVDALNVI HYMHDRYAYE RLAMALHDYP VHRYLATGIA GLSVAADSLS AIRHARVKVL
     RDESGLVTDY AIEGDFPTFG NNDDRADAIA VELVESFMAR IRRQPTYRHA EPTLSVLTLT
     SNVVYGRHTG NTPDGRRAGE PFAPDANPMN GRDRHGLVAA ALSVAKLPYD SARDGISLTS
     TVTPAGLGHT RDERVDNLVG VLDGFTDAGG FHMNVNVLDR ATLQDAMAHP ERYPQLTVRV
     SGYAVNFVRL TPEQQRDVIG RTFHGSI
//

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