ID A0A836NCC1_ECOLX Unreviewed; 555 AA. AC A0A836NCC1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-MAR-2024, entry version 10. DE SubName: Full=Hydrogenase-4 component G {ECO:0000313|EMBL:KEO29879.1}; DE EC=1.-.-.- {ECO:0000313|EMBL:KEO29879.1}; GN Name=hyfG {ECO:0000313|EMBL:KEO29879.1}; GN ORFNames=AB05_2985 {ECO:0000313|EMBL:KEO29879.1}; OS Escherichia coli 2-460-02_S1_C1. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1444044 {ECO:0000313|EMBL:KEO29879.1, ECO:0000313|Proteomes:UP000028038}; RN [1] {ECO:0000313|EMBL:KEO29879.1, ECO:0000313|Proteomes:UP000028038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-460-02_S1_C1 {ECO:0000313|EMBL:KEO29879.1, RC ECO:0000313|Proteomes:UP000028038}; RA Silbergeld E., Coles C., Seidman J.C., You Y., George J., Nadendla S., RA Daugherty S.C., Nagaraj S., Ott S., Klega K., Rasko D.; RT "Genetic Variability of E. coli after antibiotic treatment."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. 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}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KEO29879.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JOSS01000052; KEO29879.1; -; Genomic_DNA. DR RefSeq; WP_001102305.1; NZ_JOSS01000052.1. DR AlphaFoldDB; A0A836NCC1; -. DR Proteomes; UP000028038; Unassembled WGS sequence. 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, KW ECO:0000313|EMBL:KEO29879.1}. FT DOMAIN 39..155 FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit" FT /evidence="ECO:0000259|Pfam:PF00329" FT DOMAIN 297..447 FT /note="NADH-quinone oxidoreductase subunit D" FT /evidence="ECO:0000259|Pfam:PF00346" FT DOMAIN 445..523 FT /note="NADH-quinone oxidoreductase subunit D" FT /evidence="ECO:0000259|Pfam:PF00346" FT BINDING 223 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" FT BINDING 243 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" FT BINDING 246 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" FT BINDING 246 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" FT BINDING 517 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" FT BINDING 520 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1" SQ SEQUENCE 555 AA; 63380 MW; F47347A0DA67249D CRC64; MNVNSSSNRG EAILAALKTQ FPGAVLDEER QTPEQVTITV KINLLPDVVH YLYYQHDGWL PVLFGNDERT LNGHYAVYYA LSMEGAEKCW IVVKALVDAD SREFPSVTPR VPAAVWGERE IRDMYGLIPV GLPDQRRLVL PDDWPEDMHP LRKDAMDYRL RPEPTTDSET YPFINEGNSD AQVIPVGPLH ITSDELGHFR LFVDGEQIVD ADYRLFYVHR GMEKLAETRM GYNEVTFLSD RVCGICGFAH SVAYTNSVEN ALGIEVPQRA HTIRSILLEV ERLHSHLLNL GLSCHFVGFD TGFMQFFRVR EKSMTMAELL IGSRKTYGLN LIGGVRRDIL KEQRLQTLKL VREMRADVSE LVEMLLATPN MEQRTQGIGI LDRQIARDLR FDHPYADYGN IPKTLFTFTG GDVFSRVMVR VKETFDSLAM LEFALDNMPD TPLLTEGFSY KPHAFALGFV EAPRGEDVHW SMLGDNQKLF RWRCRAATYA NWPVLRYMLR GNTVSDAPLI IGSLDPCYSC TDRVTLVDVR KRQSKTVPYK EIERYGIDRN RSPLK //