AEGA_ECOLI
ID AEGA_ECOLI Reviewed; 659 AA.
AC P37127; P76560; P76970;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Putative oxidoreductase AegA {ECO:0000305};
DE AltName: Full=Anaerobically expressed gene A {ECO:0000303|PubMed:8955321};
GN Name=aegA {ECO:0000303|PubMed:8955321}; Synonyms=yffG;
GN OrderedLocusNames=b2468, JW2452;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8955321; DOI=10.1128/jb.178.23.6968-6974.1996;
RA Cavicchioli R., Kolesnikow T., Gunsalus R.P.;
RT "Characterization of the aegA locus of Escherichia coli: control of gene
RT expression in response to anaerobiosis and nitrate.";
RL J. Bacteriol. 178:6968-6974(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, INDUCTION, AND DOMAIN.
RX PubMed=30885932; DOI=10.1128/jb.00573-18;
RA Iwadate Y., Kato J.I.;
RT "Identification of a formate-dependent uric acid degradation pathway in
RT Escherichia coli.";
RL J. Bacteriol. 201:E00573-E00573(2019).
CC -!- FUNCTION: Involved in formate-dependent uric acid degradation under
CC microaerobic and anaerobic conditions. May reduce the enzymes necessary
CC for uric acid degradation. {ECO:0000269|PubMed:30885932}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AAJ3};
CC Note=Binds 5 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P0AAJ3,
CC ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- INDUCTION: Induced under anaerobic and microaerobic conditions
CC (PubMed:8955321, PubMed:30885932). This control is mediated by Fnr,
CC NarX, NarQ and NarL (PubMed:8955321). Expression is not reduced by the
CC addition of respiratory electron acceptors, including nitrate, under
CC anaerobic conditions (PubMed:30885932). {ECO:0000269|PubMed:30885932,
CC ECO:0000269|PubMed:8955321}.
CC -!- DOMAIN: Contains an N-terminal 4Fe-4S dicluster domain and a C-terminal
CC pyridine nucleotide-disulfide oxidoreductase domain.
CC {ECO:0000305|PubMed:30885932}.
CC -!- DISRUPTION PHENOTYPE: Under aerobic and anaerobic conditions, the
CC disruption mutant is able to grow utilizing ammonium, L-alanine, L-
CC arginine, L-glutamic acid, glycine, or DL-serine as the sole nitrogen
CC source. {ECO:0000269|PubMed:8955321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB46944.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L34011; AAB46944.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75521.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16342.2; -; Genomic_DNA.
DR PIR; C65022; C65022.
DR RefSeq; NP_416963.1; NC_000913.3.
DR RefSeq; WP_001078880.1; NZ_LN832404.1.
DR AlphaFoldDB; P37127; -.
DR SMR; P37127; -.
DR BioGRID; 4260929; 10.
DR DIP; DIP-9060N; -.
DR IntAct; P37127; 6.
DR STRING; 511145.b2468; -.
DR jPOST; P37127; -.
DR PaxDb; P37127; -.
DR PRIDE; P37127; -.
DR EnsemblBacteria; AAC75521; AAC75521; b2468.
DR EnsemblBacteria; BAA16342; BAA16342; BAA16342.
DR GeneID; 947383; -.
DR KEGG; ecj:JW2452; -.
DR KEGG; eco:b2468; -.
DR PATRIC; fig|1411691.4.peg.4272; -.
DR EchoBASE; EB2308; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1142; Bacteria.
DR HOGENOM; CLU_000422_3_3_6; -.
DR InParanoid; P37127; -.
DR OMA; QETQCEQ; -.
DR PhylomeDB; P37127; -.
DR BioCyc; EcoCyc:EG12409-MON; -.
DR PRO; PR:P37127; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR42783:SF1; PTHR42783:SF1; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR TIGRFAMs; TIGR01318; gltD_gamma_fam; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 5.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..659
FT /note="Putative oxidoreductase AegA"
FT /id="PRO_0000170801"
FT DOMAIN 3..22
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 47..77
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 78..107
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 114..147
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 218..252
FT /note="4Fe-4S ferredoxin-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 240
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 488
FT /note="L -> R (in Ref. 1; AAB46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="V -> A (in Ref. 1; AAB46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="W -> M (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 71844 MW; DD3ADF3E90218402 CRC64;
MNRFIMANSQ QCLGCHACEI ACVMAHNDEQ HVLSQHHFHP RITVIKHQQQ RSAVTCHHCE
DAPCARSCPN GAISHVDDSI QVNQQKCIGC KSCVVACPFG TMQIVLTPVA AGKVKATAHK
CDLCAGRENG PACVENCPAD ALQLVTDVAL SGMAKSRRLR TARQEHQPWH ASTAAQEMPV
MSKVEQMQAT PARGEPDKLA IEARKTGFDE IYLPFRADQA QREASRCLKC GEHSVCEWTC
PLHNHIPQWI ELVKAGNIDA AVELSHQTNT LPEITGRVCP QDRLCEGACT IRDEHGAVTI
GNIERYISDQ ALAKGWRPDL SHVTKVDKRV AIIGAGPAGL ACADVLTRNG VGVTVYDRHP
EIGGLLTFGI PSFKLDKSLL ARRREIFSAM GIHFELNCEV GKDVSLDSLL EQYDAVFVGV
GTYRSMKAGL PNEDAPGVYD ALPFLIANTK QVMGLEELPE EPFINTAGLN VVVLGGGDTA
MDCVRTALRH GASNVTCAYR RDEANMPGSK KEVKNAREEG ANFEFNVQPV ALELNEQGHV
CGIRFLRTRL GEPDAQGRRR PVPVEGSEFV MPADAVIMAF GFNPHGMPWL ESHGVTVDKW
GRIIADVESQ YRYQTTNPKI FAGGDAVRGA DLVVTAMAEG RHAAQGIIDW LGVKSVKSH
