ID D2TLD4_CITRI Unreviewed; 569 AA.
AC D2TLD4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Formate hydrogenlyase subunit 5 {ECO:0000313|EMBL:CBG89819.1};
GN Name=hycE {ECO:0000313|EMBL:CBG89819.1};
GN OrderedLocusNames=ROD_30901 {ECO:0000313|EMBL:CBG89819.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89819.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89819.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89819.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
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DR EMBL; FN543502; CBG89819.1; -; Genomic_DNA.
DR RefSeq; WP_012907207.1; NC_013716.1.
DR AlphaFoldDB; D2TLD4; -.
DR STRING; 637910.ROD_30901; -.
DR KEGG; cro:ROD_30901; -.
DR eggNOG; COG3261; Bacteria.
DR eggNOG; COG3262; Bacteria.
DR HOGENOM; CLU_015134_3_1_6; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR43485:SF1; FORMATE HYDROGENLYASE SUBUNIT 5-RELATED; 1.
DR PANTHER; PTHR43485; HYDROGENASE-4 COMPONENT G; 1.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR Pfam; PF00346; Complex1_49kDa; 2.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR SUPFAM; SSF143243; Nqo5-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 35..152
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 296..465
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 465..537
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 241
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 244
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 531
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 534
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 569 AA; 65112 MW; BA8FBDFBA70133EB CRC64;
MSEEKLGQHY LAALHEAFPG VVLDEAWQTR DQLTITVKVN YLPEVVEFLY YKQGGWLSVL
FGNDERQLCG HYAVYYVLSM EQGQKCWITV RVEVDPNKPE YPSVTPRVPA AVWGEREVRD
MYGLIPVGLP DERRLVLPDD WPDELYPLRK DSMDYRQRPA PTTDAETYEF INELGDKKNN
VVPIGPLHVT SDEPGHFRLF VDGENIIDAD YRLFYVHRGM EKLAETRMGY NEVTFLSDRV
CGICGFAHST AYTTSVENAM GIQVPERAQM IRAILLEVER LHSHLLNLGL ACHFTGFDSG
FMQFFRVRET SMKMAEILTG ARKTYGLNLI GGIRRDLLKD DMIQTRQLAQ QMRRDVQELV
DMLLSTPNME QRTVGIGRLD PQIARDFSNV GPMVRASGHA RDTRADHPFV GYGLLPMEVH
SEQGCDVISR LKVRINEVYT SLNMIDFGLD NLPGGPLMVE GFTYIPHRFA LGFSEAPRGD
DIHWSMTGDN QKLYRWRCRA ATYANWPTLR YMLRGNTVSD APLIIGSLDP CYSCTDRMTV
VDVRKKKSKV VPYKELERYS IERKNSPLK
//
