ID A0A0B0ENW9_9BACT Unreviewed; 682 AA.
AC A0A0B0ENW9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic {ECO:0000313|EMBL:KHE92320.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:KHE92320.1};
GN Name=ndhI {ECO:0000313|EMBL:KHE92320.1};
GN ORFNames=SCABRO_01877 {ECO:0000313|EMBL:KHE92320.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE92320.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE92320.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE92320.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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:KHE92320.1}.
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DR EMBL; JRYO01000135; KHE92320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0ENW9; -.
DR PATRIC; fig|237368.3.peg.2041; -.
DR eggNOG; COG1148; Bacteria.
DR Proteomes; UP000030652; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KHE92320.1}.
FT DOMAIN 236..265
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 599..628
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 638..667
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 682 AA; 74830 MW; 694FA446D3F0B6A6 CRC64;
MSKKIGVFVC HCGTNISATV DVEKVAEEAK KNNPGVSYTT TYKYMCSDPG QKLLRDKIKE
EGLDGVVVAA CSPKMHEHTF RNASKKAGMN PYHVEISNLR EQCSWVHPDK PTGTEKSIDL
VRMMTEKTRK DKSLNPIKVP VTKRALVIGG GIAGIQAALD IADAGHEVVM VEREASIGGH
MAQLSETFPT LDCSQCIMTP KMVELAQNEN IKLYTWSEIE AVDGYLGNFD VKIRKKARSV
DLDLCTGCSS CWQVCPSKKI KSEFDMKLGN RTAIYIPFPQ AIPSKPVIDR EHCLLFKDAR
KKNIPPNDSK VCRKCLDVCP IAPVKAIDYS QEDEIITEKI GAIVVATGYK ELDDTSMYGE
YGGGKYQDVI TGLQFERLAS ASGPTEGEIQ RPSDGKVPEI IVFIQCVGSR DPAKGCSYCS
KTCCMYTAKH TMLYKHKVHD GHAYVFYIDI RCAGKDYEEF WLRAVEEEGA TYLRGRVSRI
YKKGDKLVVL GADTLTGSVV EIEADMVVLA SAMKAQDDAE KFAQKLSIQY NKDKFFSEIH
PKLKPVESSS AGIFLAGTCQ GPKDIPETVA QAGAAASKVL ALLSADELER EPVVAKVDRL
PAPIFSTCIG CFYCKRVCPY GAIAEEDIKA RDGSVIKTVA RVNEGLCQGC GLCAATCRSK
SVELAGFNDE QVYAEINSVE FS
//
