UniProt: A0A1M4WB99

Database: UniProt
Entry: A0A1M4WB99_9BACT

LinkDB:  A0A1M4WB99_9BACT 
Original site:  A0A1M4WB99_9BACT

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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   A0A1M4WB99_9BACT        Unreviewed;       743 AA.
AC   A0A1M4WB99;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=SAMN05444362_102182 {ECO:0000313|EMBL:SHE78514.1};
OS   Dysgonomonas macrotermitis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHE78514.1, ECO:0000313|Proteomes:UP000184480};
RN   [1] {ECO:0000313|Proteomes:UP000184480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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         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; FQUC01000002; SHE78514.1; -; Genomic_DNA.
DR   RefSeq; WP_062176530.1; NZ_FQUC01000002.1.
DR   AlphaFoldDB; A0A1M4WB99; -.
DR   STRING; 1346286.SAMN05444362_102182; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000184480; 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|RuleBase:RU368075};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184480};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT   DOMAIN          1..613
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          620..743
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   REGION          604..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        405
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        406
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   MOD_RES         718
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   743 AA;  84396 MW;  69212B06DC5BCF0B CRC64;
     MDAYKDFKGT KWKEEINVND FILKNYTEYA GDESFLAGAT EATTKLWDKL SEMFKIEKEK
     GVYDAETKIP SQIDAYGPGY IDKDLEKIVG VQADKPLKRA IFPNGGLRMV QQSLEEYGYK
     LDPITTEIFS KYRKTHNEGV FSAYTDSIRR ARSNGLLTGL PDAYGRGRII GDYRRIALYG
     VDRLIAEREK RYKECDPIVM TDDLIRLREE LNSQILALKA LKRMAASYGF DISNPATNAQ
     EAVQWTYFGY LGAIKDQNGA AMSLGRVTTF LDIYIERDLK EGKITEQEAQ EIIDHFVMKL
     RIVRYLRTNE YNELFSGDPV WVTESIGGMT NNGRSMVTKN SYRMLHTLYN LGPAPEPNLT
     ILWSDRLPES WKKYCAKVSI DTSSLQYEND DIMRPQLGDD YGIACCVSPM RIGHQMQFFG
     ARANLPKALL YTINGGKDEK TKAQVLPKHW IEKVTGDYLE FDEVWDKFDR TLDWVAETYV
     KALNIIHYMH DKYSYEALEM ALHDVDIVRT QAFGVSGLSI IADSFAAIKY GKVRIVRDAD
     GDAVDYILEK DYIPFGNNDE NTDKFAVQIV EKFMNKIRKR KMYKDAIPTQ SVLTITSNVV
     YGKKTGNTPD GRRDGTPFAP GANPMHGRDT RGAVASLSSV AKLPFEHAND GISYTFAITP
     NTLGKNRDEE AQNLSGLLDG YFLQTGHHLN VNVFDRQLLI DAMEHPEQYP QLTIRVSGYA
     VNFVKLTKEQ QLDVINRTIT TTV
//

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