ID A0A0M2UQ69_9BACT Unreviewed; 611 AA.
AC A0A0M2UQ69;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=NADH dehydrogenase I subunit F {ECO:0000313|EMBL:KKO18228.1};
GN ORFNames=BROFUL_03074 {ECO:0000313|EMBL:KKO18228.1};
OS Candidatus Brocadia fulgida.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18228.1, ECO:0000313|Proteomes:UP000034954};
RN [1] {ECO:0000313|EMBL:KKO18228.1, ECO:0000313|Proteomes:UP000034954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KKO18228.1};
RX PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA Keltjens J.T., Jetten M.S.;
RT "Identification of the type II cytochrome c maturation pathway in anammox
RT bacteria by comparative genomics.";
RL BMC Microbiol. 13:265-265(2013).
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:KKO18228.1}.
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DR EMBL; LAQJ01000285; KKO18228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2UQ69; -.
DR PATRIC; fig|380242.3.peg.3800; -.
DR Proteomes; UP000034954; 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 CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
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; PF01512; Complex1_51K; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000034954};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 556..585
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 586..611
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 611 AA; 66444 MW; CD27D73EF86ECFED CRC64;
MNTTEQEKQN DGRPKIIIGM ASCGLGAGAR NVLKSIEHEL EKQKLGADIV HTGCIGMCAY
EVLVDVLFPG RTRVIYGNVK ASMVPEILGE HVGKGMAVKK FVMAQMYQGD TTAIPYEGLP
FFDELEMNRG QKKQILRNCG YIDPDSIHEY IASGGYTALS KALKTMTPKT VIDEISKSGL
RGRGGGGFPT GEKWASCAKY SADEKFVICN ADEGDPGAFM DRSLLEGDPH AVLEGMIIAG
YAINATSGYL YVRAEYPLAV KRLKHTIEEA KKLGFLGKNI LNSGYNLEIL IKEGAGAFVC
GESTSLQNSI EGKRGMPRTR PPQSVEAGLW DKPTCLNNVE TFANVPFILN KGADWYAKIG
TQNSKGTKIF SLTGKIKNAG LVEVPMGTTI RQIVFDMGGG IPKRKKFKAV QIGGPSGGCL
PESLLDSPID YESLLGAGAM MGSGSFVVVD DTTCMVEMAR FFMNFCANES CGKCPPCRIG
TTLMLEILTR ITVGEGEEKD LEVLEQMSDE MKVMSLCGLG QSAPNPVKST LRYFRDEYVA
HIRDKTCPTA TCVALHKYEV TPEKCTRCQA CIRNCPVKAI SGNTTEAAFI DKEKCIKCNL
CYEKCNFLAI K
//
