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Database: UniProt
Entry: F9Q8P0_9PAST
LinkDB: F9Q8P0_9PAST
Original site: F9Q8P0_9PAST 
ID   F9Q8P0_9PAST            Unreviewed;       576 AA.
AC   F9Q8P0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Respiratory-chain NADH dehydrogenase, 30 Kd subunit {ECO:0000313|EMBL:EGV06112.1};
GN   ORFNames=HMPREF9952_1893 {ECO:0000313|EMBL:EGV06112.1};
OS   Haemophilus pittmaniae HK 85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV06112.1, ECO:0000313|Proteomes:UP000006235};
RN   [1] {ECO:0000313|EMBL:EGV06112.1, ECO:0000313|Proteomes:UP000006235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK 85 {ECO:0000313|EMBL:EGV06112.1,
RC   ECO:0000313|Proteomes:UP000006235};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2011) 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:EGV06112.1}.
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DR   EMBL; AFUV01000010; EGV06112.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9Q8P0; -.
DR   STRING; 1035188.HMPREF9952_1893; -.
DR   Proteomes; UP000006235; 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}.
FT   DOMAIN          45..161
FT                   /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00329"
FT   DOMAIN          303..472
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          467..544
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         248
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         251
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         251
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         538
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         541
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   576 AA;  65653 MW;  6B806F3118CACDAD CRC64;
     MELTKNTSVD PAKRVGTNYI DAVNIKFPNT ILDEEWSTTN QVTLTIKTNM LPDVVSYLYY
     EHEGWLPLVF GNDERSINGH YAVYYVLSME GEVKSFVTIK ALVDPVSLEF PSVTPKVKAA
     VWGERELFDM YGLKAVGLPD QRRLVLPDDW PDDLYPLRKD SMDYRLRPDP TTATETYQFV
     NDKGDARVVP IGPLHITSDE PGHFRLFVDG EDIIDADYRL FYVHRGMEKL AEVRMDYDQV
     TFLADRVCGI CGFTHSVAYA NSVENALGIE VPIRAQWIRA ILLEVERLHS HLLNLGLSSH
     FTGFDTGFMQ FFRVREKSMT LAEVLTGARK TYGINLIGGV RRDMLKYQRE QCRKLISEMR
     TEVTNLVEIL LSTPNMEQRT VGVGILDRQV ARDFSPVGPM VRGSGFARDV RKVHPFSGYG
     DVPFNLFTEQ GCDVISRVKV RINEIFEAMN IIDYMVDNLP SGELLKEGHH FTPGRFALGI
     TEAPRGEDIH WSMLGDNQKL FRWRCRAATY ANWPALRYML RGNTVSDAPL IIGSLDPCYS
     CTDRVTVVDV RKRKAQTVAY KDIERYGIER KNSPLK
//
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