ID M1MPI0_9CLOT Unreviewed; 624 AA.
AC M1MPI0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=NADP-reducing hydrogenase subunit HndC {ECO:0000313|EMBL:AGF58128.1};
DE EC=1.12.1.3 {ECO:0000313|EMBL:AGF58128.1};
GN Name=hndC2 {ECO:0000313|EMBL:AGF58128.1};
GN ORFNames=Cspa_c43750 {ECO:0000313|EMBL:AGF58128.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF58128.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF58128.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP004121; AGF58128.1; -; Genomic_DNA.
DR RefSeq; WP_015394439.1; NZ_AOIF01000034.1.
DR AlphaFoldDB; M1MPI0; -.
DR STRING; 36745.CLSAP_41410; -.
DR KEGG; csr:Cspa_c43750; -.
DR PATRIC; fig|931276.5.peg.4407; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000011728; Chromosome.
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:0050583; F:hydrogen dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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; PF01257; 2Fe-2S_thioredx; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13237; Fer4_10; 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 Oxidoreductase {ECO:0000313|EMBL:AGF58128.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011728};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 567..596
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 597..624
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 624 AA; 68323 MW; 9E96FEB1C2857574 CRC64;
MLLNRNDLIN TRELYKKSLI KEKKKILICA GTGCVAGGSL DIYEEFIKLM KEKEINCEVS
LEKEPHDETV GIKKSGCHGF CEMGPLVRIE PFGYLYIKVK PEDCAEILEK TIINDECVER
LAYTKNGEIY KKQEEIPFYK KQTRLALEHC GHIDATSIEE YLAIDGYSAF EKVLFDMKAD
EVIKEIEESN LRGRGGGGFP AGRKWSQVSR QKEEIRYIVC NGDEGDPGAF MDRSIMEGDP
HRMLEGMMIA GVACGAQKGY IYVRAEYPLA VSRLSNAIEQ ARKYGILGEN ILGTGFSFDL
QINRGAGAFV CGEGSALTAS IEGKRGMPRV KPPRTVEQGL FGKPTVLNNV ETFANVPIVI
NKGAEWYRSI GPENSPGTKA FALTGNIENT GLIEVPMGTT LREVIFDIGG GIRDGKKFKA
VQIGGPSGGC LTAEHLDLPL DFDSLKKAGA MIGSGGLVVM DEDTCMVEVA RFFMNFTKNE
SCGKCVPCRE GTKRMLEILE GIVAGKGKLE DMDMLLELAD TISATALCGL GKTAPSPVVS
TIKNFKDEYI KHIVDKKCPS KTCQKLKTIL IDPSMCKGCS KCSKVCPVGA ISGKIKEPFV
IDQNKCIKCG ACLETCPFKA IKED
//
