ID A0A151B756_9CLOT Unreviewed; 631 AA.
AC A0A151B756;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADP-reducing hydrogenase subunit HndC {ECO:0000313|EMBL:KYH35736.1};
DE EC=1.12.1.3 {ECO:0000313|EMBL:KYH35736.1};
GN Name=hndC_1 {ECO:0000313|EMBL:KYH35736.1};
GN ORFNames=CLTEP_01290 {ECO:0000313|EMBL:KYH35736.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH35736.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH35736.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH35736.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-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:KYH35736.1}.
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DR EMBL; LTBA01000001; KYH35736.1; -; Genomic_DNA.
DR RefSeq; WP_066820995.1; NZ_LTBA01000001.1.
DR AlphaFoldDB; A0A151B756; -.
DR STRING; 1121338.CLTEP_01290; -.
DR PATRIC; fig|1121338.3.peg.131; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000075531; 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; 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; PF00037; Fer4; 2.
DR Pfam; PF10589; NADH_4Fe-4S; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KYH35736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075531}.
FT DOMAIN 575..604
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 605..631
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 631 AA; 69633 MW; 4AD8110A18204300 CRC64;
MEKIQSIGEL KELHERFKSL LVLREIPKSE NNFIKTKDFD KREVLVCAGT GCRSANSKEI
VKELNKNIIE AGLAEKVKVH ITGCFGFCEK GPIVKIYPDD VFYIKVKPDD AYEIVNKHLK
ENQIVERLLY EEPSLKQKVK TQNEMSFYKK QFRIALRNCG LINPESIDEA IGSKAYLALA
KVLTEMSPDD VIDYIYESGL RGRGGGGFLT GKKWSFAKQS NSKQKYIICN ADEGDPGAFM
DRSILEGDPH SVLEAMAIAG YAIGAYQGFI YIRAEYPLAI DRLQIAIKQA REYGLLGNNI
LGTGFNFDIS LKYGAGAFVC GEETALIHSI EGFRGEPTYK PPFPAIQGLW KKPTIVNNVE
TLANIPAIIN NGIKWFTSIG TKTSKGTKVF ALAGKINNVG LVEVPMGTTL REIIYDIGGG
IKGEAEFKAV QTGGPSGGCI PASLLDTPID YESLNEIGSM MGSGGMIVMD KNNCMVDIAK
FYLEFTLEES CGKCTPCRIG NTRLYEILDK ITKGNGTKQD LKDLEELSQI IKDTALCGLG
QTSPNPVLSN LRYFRDEFEA HINDKICPAG VCKELVRYYI TDKCIGCTRC AKICPVGCIS
GNIKEKHIID QDRCIKCGSC FEVCPVNAII K
//
