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Database: UniProt
Entry: Q32D79_SHIDS
LinkDB: Q32D79_SHIDS
Original site: Q32D79_SHIDS 
ID   Q32D79_SHIDS            Unreviewed;       571 AA.
AC   Q32D79;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Hydrogenase 4 subunit {ECO:0000313|EMBL:ABB62726.1};
GN   Name=hyfG {ECO:0000313|EMBL:ABB62726.1};
GN   OrderedLocusNames=SDY_2676 {ECO:0000313|EMBL:ABB62726.1};
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB62726.1, ECO:0000313|Proteomes:UP000002716};
RN   [1] {ECO:0000313|EMBL:ABB62726.1, ECO:0000313|Proteomes:UP000002716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197 {ECO:0000313|EMBL:ABB62726.1,
RC   ECO:0000313|Proteomes:UP000002716};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62726.1; -; Genomic_DNA.
DR   RefSeq; WP_001102278.1; NC_007606.1.
DR   RefSeq; YP_404217.1; NC_007606.1.
DR   AlphaFoldDB; Q32D79; -.
DR   STRING; 300267.SDY_2676; -.
DR   EnsemblBacteria; ABB62726; ABB62726; SDY_2676.
DR   KEGG; sdy:SDY_2676; -.
DR   PATRIC; fig|300267.13.peg.3228; -.
DR   HOGENOM; CLU_015134_3_1_6; -.
DR   Proteomes; UP000002716; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002716}.
FT   DOMAIN          39..155
FT                   /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00329"
FT   DOMAIN          297..463
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          461..539
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         533
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         536
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   571 AA;  64997 MW;  A387D2F24E3CDCCB CRC64;
     MNVNSSSNRG EAILAALKTQ FPGAVLDEDR QTPEQVTITV KINLLPDVVQ YLYYQHDGWL
     PVLFGNDERT LNGHYAVYYA LSMEGAEKCW IVVKALVNAD SREFPSVTPH VPAAVWGERE
     IRDMYGLIPV GLPDQRRLVL PDDWPEDMHP LRKDAMDYRL RPEPTTDSET YPFINEGNSD
     ARVIPVGPLH ITSDEPGHFR LFVDGEQIVD ADYRLFYVHR GMEKLAETRM GYNEVTFLSD
     RVCGICGFAH SVAYTNSVEN ALGIEVPQRA HTIRSILLEV ERLHSHLLNL GLSCHFVGFD
     TGFMQFFRVR EKSMTMAELL TGSRKTYGLN LIGGVRRDIL KEQRLQTLKL VREIRADVSV
     LVEMLFATPN MEQRTQGIGI LDRQIARDYS PVGPLIRGSG FARDLRFDHP YADYGNIPKT
     LFTFTGGDVF SRVMVRVKET FDSLAMLEFA LDNMPDTPLL TEGFSYKPHA FALGFVEAPR
     GEDVHWSMLG DNQKLFRWRC RAATYANWPV LRYMLRGNTV SDAPLIIGSL DPCYSCTDRV
     TLVDVRKRQS KTVPYKEIER YGIDRNRSPL K
//
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