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Database: UniProt
Entry: A0A1T2KWB5_9GAMM
LinkDB: A0A1T2KWB5_9GAMM
Original site: A0A1T2KWB5_9GAMM 
ID   A0A1T2KWB5_9GAMM        Unreviewed;       591 AA.
AC   A0A1T2KWB5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NADP oxidoreductase {ECO:0000313|EMBL:OOZ37147.1};
GN   ORFNames=BOW51_03830 {ECO:0000313|EMBL:OOZ37147.1};
OS   Solemya velesiana gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918948 {ECO:0000313|EMBL:OOZ37147.1, ECO:0000313|Proteomes:UP000190896};
RN   [1] {ECO:0000313|EMBL:OOZ37147.1, ECO:0000313|Proteomes:UP000190896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Se-Cadez {ECO:0000313|EMBL:OOZ37147.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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:OOZ37147.1}.
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DR   EMBL; MPRJ01000017; OOZ37147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2KWB5; -.
DR   OrthoDB; 9805533at2; -.
DR   Proteomes; UP000190896; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR041921; NuoE_N.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190896}.
FT   DOMAIN          469..514
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   591 AA;  65056 MW;  858EB6B08FBAE770 CRC64;
     MTDDHITETT NRVMTQWNND QSNLLQMLID LQQALNGIPE SAINQISAGT RRSPADIESV
     IGFYSFLHHD THNPYRVLFS DNITDRMLGS RALAEHLNSR LQDIDTATVD YTSCTGMGDQ
     GPAALVNGHT LTRLDKERID QMAALMETNT PLSDWPAEWF RVDENIRRRD LLLETDFEKG
     SAIKCALESG AEKILEELDA SGLRGRGGAG FKTAMKWRFC REATGDNRVV VCNADEGEPG
     TFKDRLLLQS FAERLIEGMT VCAKVIGATT GFIYLRGEYL YLRDELESKL QRYRDAGLLS
     KDIHGEAGFD FDIKIHLGAG AYICGEESAL IESLEGKRGI PRIRPPFPVT SGYLNRPTVV
     NNVETLVAAA MIAVHGAAWF RTKGTEQSPG TKLLSISGNC LKPGIYEYPF GTSLEVILKD
     CEATHVQAVQ IAGAAGSCIP PSEFSRSIAF EDLATGGSFM IFDRERNLLE MVQNFTDFFV
     HESCGFCTPC RVGTSLLKKR LAKVASGRAT GVDLEKMRII GSLTRQTSHC GLGMTAANPI
     LETLDKFPHI YEPHLLSTTF EPAFNLDASL EEARQITGRD DPDAHLQGGG V
//
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