ETFQR_SYNWW
ID ETFQR_SYNWW Reviewed; 714 AA.
AC Q0AZ32;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=EtfAB:quinone oxidoreductase {ECO:0000303|PubMed:23468890};
DE EC=1.18.-.- {ECO:0000305|PubMed:23468890};
GN OrderedLocusNames=Swol_0698 {ECO:0000312|EMBL:ABI68022.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=19648244; DOI=10.1128/jb.01605-08;
RA Mueller N., Schleheck D., Schink B.;
RT "Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A
RT dehydrogenase in reversed electron transport during syntrophic butyrate
RT oxidation by Syntrophomonas wolfei.";
RL J. Bacteriol. 191:6167-6177(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP FUNCTION, AND PATHWAY.
RX PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA Schmidt A., Mueller N., Schink B., Schleheck D.;
RT "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT Syntrophomonas wolfei.";
RL PLoS ONE 8:E56905-E56905(2013).
CC -!- FUNCTION: Oxidoreductase involved in syntrophic growth of S.wolfei with
CC butyrate. Is presumed to link the electron flow from butyryl-CoA
CC dehydrogenases to the membrane, in conjunction with the electron
CC transfer flavoprotein EtfAB. May transfer electrons to the menaquinone
CC pool of the membrane. {ECO:0000305|PubMed:19648244,
CC ECO:0000305|PubMed:23468890}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00711};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC -!- SUBUNIT: Might constitute a membrane-associated complex with EtfA
CC (Swol_0697), EtfB (Swol_0696), and the butyryl-CoA dehydrogenase
CC Swol_1933 and/or Swol_2052. {ECO:0000305|PubMed:19648244,
CC ECO:0000305|PubMed:23468890}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23468890};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC protein level) (PubMed:19648244, PubMed:23468890). Seems to be
CC constitutively expressed (PubMed:23468890).
CC {ECO:0000269|PubMed:19648244, ECO:0000269|PubMed:23468890}.
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DR EMBL; CP000448; ABI68022.1; -; Genomic_DNA.
DR RefSeq; WP_011640127.1; NC_008346.1.
DR AlphaFoldDB; Q0AZ32; -.
DR STRING; 335541.Swol_0698; -.
DR EnsemblBacteria; ABI68022; ABI68022; Swol_0698.
DR KEGG; swo:Swol_0698; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG2181; Bacteria.
DR HOGENOM; CLU_005304_1_0_9; -.
DR OMA; SGCPYCL; -.
DR OrthoDB; 1951488at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Fatty acid metabolism; Iron; Iron-sulfur;
KW Lipid metabolism; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..714
FT /note="EtfAB:quinone oxidoreductase"
FT /id="PRO_0000442216"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 293..324
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 375..405
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 305
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 386
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 389
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 392
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 396
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 714 AA; 81418 MW; 932B269577829394 CRC64;
MIFGFHPLEG GYDVPMRVVG ANIPYEWLIY VIMLIPVSVF LFGFWKKLEV WLLAKGEIHR
NDKIAQRIWS WFVFSFAQAR VIRKPLAGWM HAFLFWGFLV LFLAAGIDAM HNMISWPHLE
GNFYIGFSWV VDVLGFLALI GVMVLGFVRY FQKPERLNDT KSSDGWIILL IFAILLTGYF
IEGLRIAAQI KLSTTMQQIA YERAASPFGW MFASFFGSMS VDAMLMWHRL LWWFHMAIAF
LFIALVPFTK LWHIFASMLN YTFRDLEPSA NRMVYNIEEA ETFGVENIED FGWKDLLDLD
SCIRCGRCQE NCPAYNTGKH LNPKITLIQN MKAHLDAKAP YLLAAKASGA EVEEMAMTEE
AAAEEVNPME QSLLYDVVGS ETIWDCTNCR ACMEHCPMFI EHIPKIVEMR RNLVMWQGDM
PGEAQMAFTN MERNYNPWGV GWAGRAGWLD ERGVREMVNL LPEDGKEFEY LLYAGCAVSF
DDRYKRVGEA LVRLLNKAGV SFGYLGTEEY CCGDSARRLG NEYLYQTLVS QNLESFNNYG
VKKIIVVCPH GYTALKNEYP QMGGNYEVYH YTEILAKLVA EGKLKPSKPL GVKMTYHDSC
FLGRHNGVYD QPRNVLKAAG GQVIEIEKAK EFGFCCGAGG GRMWLEEEAV LKDGIQYKRI
NDTRTDQLLV PNPEMIVTNC PFCLTMIADG VKAAEAEEST KVFDVAEVLW KAME
