ID A0A162TBV1_9CLOT Unreviewed; 562 AA.
AC A0A162TBV1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=NADP-reducing hydrogenase subunit HndC {ECO:0000313|EMBL:KZL92444.1};
DE EC=1.12.1.3 {ECO:0000313|EMBL:KZL92444.1};
GN Name=hndD_3 {ECO:0000313|EMBL:KZL92444.1};
GN ORFNames=CLMAG_22530 {ECO:0000313|EMBL:KZL92444.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL92444.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL92444.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL92444.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KZL92444.1}.
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DR EMBL; LWAE01000002; KZL92444.1; -; Genomic_DNA.
DR RefSeq; WP_066621929.1; NZ_LWAE01000002.1.
DR AlphaFoldDB; A0A162TBV1; -.
DR STRING; 1121326.CLMAG_22530; -.
DR PATRIC; fig|1121326.3.peg.2249; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000076603; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR02512; FeFe_hydrog_A; 1.
DR PANTHER; PTHR11615:SF6; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
PE 4: Predicted;
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:KZL92444.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603}.
FT DOMAIN 2..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 79..118
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 138..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..210
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 562 AA; 61806 MW; A3190AD6CC5C5169 CRC64;
MSRQFMTIDN VPVEIKGEKN ILELVRREGI DLPTFCFYSE LSVYGACRMC MVETKRGGME
AACSTPPKAG MEIFTNTPRL RKYRKNILEL LLANHCRDCT TCEKSGRCRL QYLAKRFGIK
KVRFENSSNK NLIDDSSVSI VRDQSKCILC GDCVRVCEEV QNVGVIDFAH RGSKMTVTTA
FDEPIGDSNC VSCGQCAAVC PTGAIVVKSN TDKLWNELSD KNTQVVVQVA PAVRVAITSE
LGQGNGQNSM GKIVAALRKM GFDKVFDTSV SADLTVIEET NEFIGKLQQK ENLPLFSSCC
PGWINYVENF HPELLNKNIS SCKSPMQMFA AVLKDYYKSD DKKLVSVAIM PCSAKKYEAT
REEFKRNGVP DVDYVVTTQE LINMIKESGI VFSELEPEAV DMPFDLSSGA GVIFGVTGGV
TEAVMRKVLS DQPISVVRSL AFETVRGMDG VKEAALTVGD REIKVAVVSG LKNADDVIKK
IKSGEAHYDF VEVMACPGGC VAGAGQPFAK DGGKLKRGDG LYQADKMTSI SRADDNPLME
KLYSGILKDR VHELLHVHYH VK
//
