ID A0A1V4I526_9FIRM Unreviewed; 597 AA.
AC A0A1V4I526;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NADP-reducing hydrogenase subunit HndC {ECO:0000313|EMBL:OPJ54970.1};
DE EC=1.12.1.3 {ECO:0000313|EMBL:OPJ54970.1};
GN Name=hndC_3 {ECO:0000313|EMBL:OPJ54970.1};
GN ORFNames=CLOTH_17820 {ECO:0000313|EMBL:OPJ54970.1};
OS [Clostridium] thermoalcaliphilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=29349 {ECO:0000313|EMBL:OPJ54970.1, ECO:0000313|Proteomes:UP000190140};
RN [1] {ECO:0000313|EMBL:OPJ54970.1, ECO:0000313|Proteomes:UP000190140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7309 {ECO:0000313|EMBL:OPJ54970.1,
RC ECO:0000313|Proteomes:UP000190140};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium thermoalcaliphilum DSM 7309.";
RL Submitted (MAR-2017) 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:OPJ54970.1}.
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DR EMBL; MZGW01000009; OPJ54970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4I526; -.
DR STRING; 29349.CLOTH_17820; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000190140; 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: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; PF14697; Fer4_21; 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; 2.
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:OPJ54970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190140};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 540..569
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 570..597
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 597 AA; 64817 MW; 7F5622631445CD36 CRC64;
MAYKNEVLVC GGTGCISSSS LKILDKMENL LAEKGMKDDV KLIKTGCFGL CAAGPIVIVY
PEGAFYSQVQ LEDVEKIVDE HIVGGKVVKE LLYKEALTED GEMKPFEEVP FYKKQERVAL
RNCGAIGAES IEDYLARDGY KALEKVLKEM SQEEVIDVVK RSGLRGRGGG GFPTGLKWEF
TYKAQDDQKY VACNADEGDP GAFMDRSILE GDPHALVEAM AIAGYAVGAN MGYVYVRAEY
PTAVERLQIA IDTAREKGIL GKDIFGTGFE FDMEIRLGAG AFVCGEETAL INSIEGRRGM
PRPRPPFPAV KGIWNKPTLL NNVETYANIP RIILNGPEWF AAMGTEKSKG TKVFALGGKV
NNVGLVEIPM GTTLREIIFE VGGGIPNGKK FKAVQTGGPS GGCLTEEYLD TQIDYDTLTA
LGSMMGSGGM VVMDEDNCMV DIAKFFLDFT VEESCGKCPP CRIGTKRMLE ILDRITEGHG
ELEDLNRLEK LANSIKSAAL CGLGQTAPNP VLSTLNHFRA EYEAHVVDKK CPSGVCQELL
QFSILEDKCK GCTLCVKACP VNAISGERKA LHSIDTNACV KCGACIEKCP FKAIIKK
//
