UniProt: A0A0E4C8M9

Database: UniProt
Entry: A0A0E4C8M9_9FIRM

LinkDB:  A0A0E4C8M9_9FIRM 
Original site:  A0A0E4C8M9_9FIRM

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

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ID   A0A0E4C8M9_9FIRM        Unreviewed;       744 AA.
AC   A0A0E4C8M9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Formate acetyltransferase {ECO:0000256|ARBA:ARBA00013897, ECO:0000256|RuleBase:RU368075};
DE            EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214, ECO:0000256|RuleBase:RU368075};
DE   AltName: Full=Pyruvate formate-lyase {ECO:0000256|ARBA:ARBA00031063, ECO:0000256|RuleBase:RU368075};
GN   ORFNames=1417 {ECO:0000313|EMBL:CFX54346.1};
OS   Syntrophomonas zehnderi OL-4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX54346.1, ECO:0000313|Proteomes:UP000045545};
RN   [1] {ECO:0000313|EMBL:CFX54346.1, ECO:0000313|Proteomes:UP000045545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL-4 {ECO:0000313|EMBL:CFX54346.1,
RC   ECO:0000313|Proteomes:UP000045545};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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|ARBA:ARBA00004809,
CC       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; CGIH01000026; CFX54346.1; -; Genomic_DNA.
DR   RefSeq; WP_046497005.1; NZ_CGIH01000026.1.
DR   AlphaFoldDB; A0A0E4C8M9; -.
DR   STRING; 690567.1417; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000045545; Unassembled WGS sequence.
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|ARBA:ARBA00022526,
KW   ECO:0000256|RuleBase:RU368075};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000045545};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT   DOMAIN          1..614
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          621..744
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   ACT_SITE        408
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        409
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   MOD_RES         719
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   744 AA;  84607 MW;  E58F9FAB9F13AD85 CRC64;
     MQNTAWEGFV AGHWVDEIDV RDFIQLNYMP YTGDGTFLKP PTAKSLDLWD KVKKLLWEEH
     QKNGVLNIDT HTVSSITSHK PCYIDRDLEV IVGLQTDEPL KRAIMPMGGI RMVRAATDSY
     GYELDPEIDL IFTHYRKTHN QGVFDVYTPE IRKARKAGII TGLPDAYGRG RIIGDYRRIA
     LYGTDFLIKN KIACLKQIEY DVFTDDLIRL REEVSEQITA LKELNEMAEM YGYDISQPAR
     NAREAVQFVY FGYLGSIKEQ NGAAMSLGRV STFLDIYLNR DLKRGDIDEE AAQELIDQFC
     IKLRMVRFLR TVDYNELFSG DPVWVTESIG GMGIDGRTLV TRTSFRFLHT LNNLGSAPEP
     NLTVLWSQNL PQPFKEFCAQ TSIDTSSIQY ENDDLMRPYW GDDYAIACCV SAMRIGKQMQ
     YFGARANLAK ALLYAINGGI DEMLGLQVAP EFKPISGDIL DYDELWDRYD KVLEWLAKTY
     VNTMNIIHYM HDKYAYERLE FALHDLNIYR TMAFGMAGLS VVADSLSAVK HARVKIIRNS
     QGLATDFEVC GEYPSFGNND PRVDEIAILV QKTFMEKLAK HPTYRDSKHT LSILTITSNV
     VYGKKTGSTP DGRKAGEPFA PGANPMHGRD QRGALASMNS VAKLPYRYAL DGISYTFSII
     PKALGREIKE RPRNLRSLLD GYFASGGHHI NVNVLEREIL EDAIEHPEKY PQLTIRVSGY
     AVNFIKLTRE QQLDVINRTF HTIV
//

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