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HYDN_ECOLI
ID   HYDN_ECOLI              Reviewed;         175 AA.
AC   P0AAK4; P30132; Q2MAB6;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Electron transport protein HydN;
GN   Name=hydN; OrderedLocusNames=b2713, JW2683;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Ikebukuro K., Nishio M., Yano K., Tomiyama M., Tamiya E., Karube I.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=8661925; DOI=10.1007/s002030050335;
RA   Maier T., Binder U., Boeck A.;
RT   "Analysis of the hydA locus of Escherichia coli: two genes (hydN and hypF)
RT   involved in formate and hydrogen metabolism.";
RL   Arch. Microbiol. 165:333-341(1996).
CC   -!- FUNCTION: Electron transport from formate to hydrogen.
CC       {ECO:0000269|PubMed:8661925}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
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DR   EMBL; D14422; BAA03314.1; -; Genomic_DNA.
DR   EMBL; U29579; AAA69223.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75755.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76790.1; -; Genomic_DNA.
DR   PIR; E65051; E65051.
DR   RefSeq; NP_417193.1; NC_000913.3.
DR   RefSeq; WP_001078777.1; NZ_STEB01000027.1.
DR   AlphaFoldDB; P0AAK4; -.
DR   SMR; P0AAK4; -.
DR   BioGRID; 4259425; 21.
DR   BioGRID; 851522; 11.
DR   IntAct; P0AAK4; 13.
DR   STRING; 511145.b2713; -.
DR   PaxDb; P0AAK4; -.
DR   PRIDE; P0AAK4; -.
DR   EnsemblBacteria; AAC75755; AAC75755; b2713.
DR   EnsemblBacteria; BAE76790; BAE76790; BAE76790.
DR   GeneID; 67413990; -.
DR   GeneID; 947190; -.
DR   KEGG; ecj:JW2683; -.
DR   KEGG; eco:b2713; -.
DR   PATRIC; fig|1411691.4.peg.4029; -.
DR   EchoBASE; EB1513; -.
DR   eggNOG; COG1142; Bacteria.
DR   HOGENOM; CLU_043374_3_0_6; -.
DR   InParanoid; P0AAK4; -.
DR   OMA; ILCRLCM; -.
DR   PhylomeDB; P0AAK4; -.
DR   BioCyc; EcoCyc:EG11552-MON; -.
DR   PRO; PR:P0AAK4; -.
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:0009055; F:electron transfer activity; IMP:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12800; Fer4_4; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..175
FT                   /note="Electron transport protein HydN"
FT                   /id="PRO_0000159269"
FT   DOMAIN          2..32
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          48..79
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          80..109
FT                   /note="4Fe-4S ferredoxin-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          124..157
FT                   /note="4Fe-4S ferredoxin-type 4"
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"
FT   BINDING         15
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   175 AA;  19026 MW;  CB2A1C52BF6A558E CRC64;
     MNRFIIADAS KCIGCRTCEV ACVVSHQENQ DCASLTPETF LPRIHVIKGV NISTATVCRQ
     CEDAPCANVC PNGAISRDKG FVHVMQERCI GCKTCVVACP YGAMEVVVRP VIRNSGAGLN
     VRADKAEANK CDLCNHREDG PACMAACPTH ALICVDRNKL EQLSAEKRRR TALMF
 
 
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