ID   A0A836NCC1_ECOLX        Unreviewed;       555 AA.
AC   A0A836NCC1;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   03-MAY-2023, entry version 7.
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}.
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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   GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
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:0000313|EMBL:KEO29879.1}.
FT   DOMAIN          42..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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         517
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         520
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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
//