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Database: UniProt
Entry: A0A1S8T8V0_9CLOT
LinkDB: A0A1S8T8V0_9CLOT
Original site: A0A1S8T8V0_9CLOT 
ID   A0A1S8T8V0_9CLOT        Unreviewed;       709 AA.
AC   A0A1S8T8V0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADPH-Fe(3+) oxidoreductase subunit beta {ECO:0000313|EMBL:OOM74082.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:OOM74082.1};
GN   Name=sfrB_1 {ECO:0000313|EMBL:OOM74082.1};
GN   ORFNames=CLPUN_41430 {ECO:0000313|EMBL:OOM74082.1};
OS   Clostridium puniceum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM74082.1, ECO:0000313|Proteomes:UP000190890};
RN   [1] {ECO:0000313|EMBL:OOM74082.1, ECO:0000313|Proteomes:UP000190890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM74082.1,
RC   ECO:0000313|Proteomes:UP000190890};
RA   Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA   Daniel R.;
RT   "Microbial solvent formation.";
RL   Submitted (MAY-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:OOM74082.1}.
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DR   EMBL; LZZM01000204; OOM74082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8T8V0; -.
DR   STRING; 29367.CLPUN_41430; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000190890; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
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; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
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:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:OOM74082.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190890}.
FT   DOMAIN          2..78
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          78..117
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          137..170
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          181..209
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   709 AA;  78057 MW;  E3F9249EA348B48E CRC64;
     MKDIKITIDG KEIITKEGKN VLDCALESGI YIPHLCHHPD LPELGACRLC VVEHNGEIVT
     SCTLKAEDGM AIKTQNEQIN KKRQLAMELI LAAHPEECST CTKYGKCELQ VLIQYLGVGP
     ERLRMRVKPF PKNTSNQLFD HDMTRCVLCG RCARVCQKVR KVNAIDYQKK NSEVYIGTPH
     EKLLIDADCK FCGACVEICP TGALMDKKEL VDLNKNKDTS LVPCRNTCPA GTNIPTYIRL
     VNEGKYSEAT AVIREKLPIP KILGHICSHP CESECRRGNV NEAVSIRELK LFAVEHDEKE
     IWKKNRKLLP ATGKKVGVIG AGPAGLSAAY YLKKQGHDVT VYEALPYAGG MTRVGIPEYR
     MPRNIIEEEV NLIKEIGVEI VTNTKVEKFE SLLNDGYDAV LTAIGAHKGV RLPIEGNDLE
     GVLLNSDFLR AVSLNEEVKI GEKVIVLGGG NVAFDCARTA VRLGAKKVHL ACLENEQNIP
     ASEDEVKAGI EEGITIHYSK SFAKILGEED KIAGIEFVNV ESMSFDENRR LTINLVEGSN
     HILEVDQIIF ATGQRPDIDE SSGFELGRGN TIVVNDMQET NKKGIFAAGD AIYGTNSVVK
     AVASGRDAAK AIDKFLGGDG NIDEHLIDVD EPNKCIGKKA GFGYEERIIP SEVDVNSRKT
     NFSRAENGFT CEQADKESSR CLQCDLRLGI SKPKTWNDFA GITIERGNE
//
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