UACF_ECOLI
ID UACF_ECOLI Reviewed; 639 AA.
AC Q46820; Q2M9V4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Putative oxidoreductase UacF {ECO:0000305};
DE AltName: Full=Uric acid degradation formate-related element {ECO:0000303|PubMed:30885932};
GN Name=uacF {ECO:0000303|PubMed:30885932}; Synonyms=ygfT;
GN OrderedLocusNames=b2887, JW5469;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 Expression increases in the presence of hypoxanthine, xanthine and uric
CC acid. Expression is reduced in the presence of nitrite and nitrate
CC under anaerobic conditions. {ECO:0000269|PubMed:30885932}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA83068.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28375; AAA83068.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75925.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76952.1; -; Genomic_DNA.
DR PIR; G65072; G65072.
DR RefSeq; NP_417363.2; NC_000913.3.
DR RefSeq; WP_001350545.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46820; -.
DR SMR; Q46820; -.
DR BioGRID; 4262335; 15.
DR DIP; DIP-12175N; -.
DR STRING; 511145.b2887; -.
DR PaxDb; Q46820; -.
DR PRIDE; Q46820; -.
DR EnsemblBacteria; AAC75925; AAC75925; b2887.
DR EnsemblBacteria; BAE76952; BAE76952; BAE76952.
DR GeneID; 949018; -.
DR KEGG; ecj:JW5469; -.
DR KEGG; eco:b2887; -.
DR PATRIC; fig|1411691.4.peg.3848; -.
DR EchoBASE; EB2881; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1142; Bacteria.
DR HOGENOM; CLU_000422_3_3_6; -.
DR InParanoid; Q46820; -.
DR OMA; DRANMPG; -.
DR PhylomeDB; Q46820; -.
DR BioCyc; EcoCyc:G7506-MON; -.
DR PRO; PR:Q46820; -.
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..639
FT /note="Putative oxidoreductase UacF"
FT /id="PRO_0000170802"
FT DOMAIN 3..32
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 110..139
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 201..235
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 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 639 AA; 69089 MW; 3B2B96621835655C CRC64;
MNKFIAAEAA ECIGCHACEI ACAVAHNQEN WPLSHSDFRP RIHVVGKGQA ANPVACHHCN
NAPCVTACPV NALTFQSDSV QLDEQKCIGC KRCAIACPFG VVEMVDTIAQ KCDLCNQRSS
GTQACIEVCP TQALRLMDDK GLQQIKVARQ RKTAAGKASS DAQPSRSAAL LPVNSRKGAD
KISASERKTH FGEIYCGLDP QQATYESDRC VYCAEKANCN WHCPLHNAIP DYIRLVQEGK
IIEAAELCHQ TSSLPEICGR VCPQDRLCEG ACTLKDHSGA VSIGNLERYI TDTALAMGWR
PDVSKVVPRS EKVAVIGAGP AGLGCADILA RAGVQVDVFD RHPEIGGMLT FGIPPFKLDK
TVLSQRREIF TAMGIDFHLN CEIGRDITFS DLTSEYDAVF IGVGTYGMMR ADLPHEDAPG
VIQALPFLTA HTRQLMGLPE SEEYPLTDVE GKRVVVLGGG DTTMDCLRTS IRLNAASVTC
AYRRDEVSMP GSRKEVVNAR EEGVEFQFNV QPQYIACDED GRLTAVGLIR TAMGEPGPDG
RRRPRPVAGS EFELPADVLI MAFGFQAHAM PWLQGSGIKL DKWGLIQTGD VGYLPTQTHL
KKVFAGGDAV HGADLVVTAM AAGRQAARDM LTLFDTKAS
