ID Q2RXM4_RHORT Unreviewed; 561 AA.
AC Q2RXM4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=NADH-ubiquinone oxidoreductase {ECO:0000313|EMBL:ABC21121.1};
DE EC=1.6.5.3 {ECO:0000313|EMBL:ABC21121.1};
GN OrderedLocusNames=Rru_A0316 {ECO:0000313|EMBL:ABC21121.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC21121.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC21121.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC21121.1; -; Genomic_DNA.
DR RefSeq; WP_011388069.1; NC_007643.1.
DR RefSeq; YP_425408.1; NC_007643.1.
DR AlphaFoldDB; Q2RXM4; -.
DR STRING; 269796.Rru_A0316; -.
DR EnsemblBacteria; ABC21121; ABC21121; Rru_A0316.
DR KEGG; rru:Rru_A0316; -.
DR PATRIC; fig|269796.9.peg.372; -.
DR eggNOG; COG3261; Bacteria.
DR HOGENOM; CLU_015134_3_1_5; -.
DR PhylomeDB; Q2RXM4; -.
DR Proteomes; UP000001929; 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; IPR020396; NADH_UbQ_OxRdtase_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; PS00542; COMPLEX1_30K; 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:ABC21121.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929}.
FT DOMAIN 34..150
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 290..454
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 463..532
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 236
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 239
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 526
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 529
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 561 AA; 62706 MW; D82E5A5535AE32BC CRC64;
MTTPQTILDD INARFPGCVT RGLAPQPDRL YLRTTTEHIR TLAAYVFNDL KGRLVTGVCT
DMGPVTGEYD IIYAFSLDAE GILLTLTEPT DPKDPKVPTL TDLIPGADWH ERENYDMLGV
VAEGHPNPRR LLLSEDWPED LFPMRKDFPH DFKPPKAEKI TTPLRDPLGN ESKATIISVG
PFFPTLDEPA YFRLFCEGEE IIGSDYRGFF SHRGIEKLSD TVLDYNQVPF MAERVCGICG
FVHSACYCMA VEDAAGIEIP PRAKYIRSIM MELERLHSHL LWLGLAGHYL GFDTVLMQSW
RIREPIMWLV EEITGNRKTY GMNLVGGVRR DLDSAICDKI MAAVTKIGIE CEELISAVAG
DESLKMRMVK VGVLSHEDAR GICVVGPTAR ASGVHIDARA DYPYAAFPDL DFKPSFHEGG
DIWARTLVRV DEVRSSVDLI KQMITKLPEG EIMAGFGPIP AWREGYGIAE APRGECVHYV
QTGKDNRPYR WRVRAATYPQ LQAVPLMLKG MSIGDFPIII GSIDPCFSCT ERVLTVDTKS
KAIRTYTEKD LLALTRRAGG R
//
