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Database: UniProt
Entry: D4H7J5_DENA2
LinkDB: D4H7J5_DENA2
Original site: D4H7J5_DENA2 
ID   D4H7J5_DENA2            Unreviewed;       318 AA.
AC   D4H7J5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=4Fe-4S ferredoxin iron-sulfur binding domain protein {ECO:0000313|EMBL:ADD67994.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Dacet_1222 {ECO:0000313|EMBL:ADD67994.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67994.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD67994.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036298-50};
CC       Note=Binds 4 [4Fe-4S] clusters per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036298-50};
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DR   EMBL; CP001968; ADD67994.1; -; Genomic_DNA.
DR   RefSeq; WP_013010516.1; NC_013943.1.
DR   AlphaFoldDB; D4H7J5; -.
DR   STRING; 522772.Dacet_1222; -.
DR   PaxDb; 522772-Dacet_1222; -.
DR   KEGG; dap:Dacet_1222; -.
DR   eggNOG; COG0437; Bacteria.
DR   HOGENOM; CLU_043374_0_0_0; -.
DR   InParanoid; D4H7J5; -.
DR   OrthoDB; 9789030at2; -.
DR   Proteomes; UP000002012; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR   GO; GO:0015944; P:formate oxidation; IEA:InterPro.
DR   CDD; cd10561; HybA_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014603; Formate_DH_Fe-S_su.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43545; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR43545:SF1; HYDROGENASE-2 OPERON PROTEIN HYBA; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036298-
KW   50};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036298-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..318
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003058038"
FT   DOMAIN          39..69
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          99..132
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          134..163
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         110
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         118
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         122
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         143
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         146
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         172
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         175
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         192
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
SQ   SEQUENCE   318 AA;  35873 MW;  5582AF8E0C0396EA CRC64;
     MKKTRRDFLK SAAAGGALVA APFSLHAEEE HLKESDEAVG MLYDSTLCVG CKACVTKCKQ
     VNDMEAVPSP SDEDRIWDSP EDLDYRTRNI IKLYKDKENE ANWDYVKYQC MHCIKPSCVS
     ACPVSAMEQE KERGIVFYDK NKCIGCRYCQ IACPFNIPKF GWPETFPKIV KCDLCKYTNL
     KVKGEPACVE TCPTQAVIYG KRKDLLAEAK RRLVTSPEKY TGEIYGEYEV GGTNVLYLAG
     TDFSNLGFPE LEKESAAVRS EHIQHTLYKG FIAPVALYGF LAMVALKNRK TAQQVEKEHV
     IEKEIETELK HEDEGGDK
//
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