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Database: UniProt
Entry: F3KRF9_9BURK
LinkDB: F3KRF9_9BURK
Original site: F3KRF9_9BURK 
ID   F3KRF9_9BURK            Unreviewed;       304 AA.
AC   F3KRF9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Formate dehydrogenase subunit beta {ECO:0000313|EMBL:EGI77649.1};
GN   ORFNames=HGR_05181 {ECO:0000313|EMBL:EGI77649.1};
OS   Hylemonella gracilis ATCC 19624.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hylemonella.
OX   NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77649.1, ECO:0000313|Proteomes:UP000016368};
RN   [1] {ECO:0000313|EMBL:EGI77649.1, ECO:0000313|Proteomes:UP000016368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77649.1,
RC   ECO:0000313|Proteomes:UP000016368};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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};
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:EGI77649.1}.
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DR   EMBL; AEGR01000043; EGI77649.1; -; Genomic_DNA.
DR   RefSeq; WP_006297042.1; NZ_AEGR01000043.1.
DR   AlphaFoldDB; F3KRF9; -.
DR   STRING; 887062.HGR_05181; -.
DR   eggNOG; COG0437; Bacteria.
DR   OrthoDB; 9779457at2; -.
DR   Proteomes; UP000016368; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd10558; FDH-N; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 1.20.5.480; Single helix bin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR006470; Formate_DH_bsu_Proteobacteria.
DR   InterPro; IPR038384; Formate_DH_C_sf.
DR   InterPro; IPR014603; Formate_DH_Fe-S_su.
DR   InterPro; IPR015246; Formate_DH_TM.
DR   NCBIfam; TIGR01582; FDH-beta; 1.
DR   PANTHER; PTHR43545; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR43545:SF4; FORMATE DEHYDROGENASE-O IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12800; Fer4_4; 1.
DR   Pfam; PF09163; Form-deh_trans; 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.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036298-
KW   50}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036298-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016368};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          30..60
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          93..125
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          126..155
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         42
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         49
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
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         114
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         135
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         138
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         141
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         145
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         165
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         177
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         181
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
SQ   SEQUENCE   304 AA;  33161 MW;  8289397FEFA22691 CRC64;
     MSSLQSLDIR RRSATTTPSP SIREAHSGEV AKLIDVSKCI GCKACQTACM EWNDLREEVG
     SNHGVYDNPM DLTEHSWTVM RFTEYENTAT GNLEWLIRKD GCMHCADPGC LKACPSPGAI
     VQYANGIVDF QEEHCIGCGY CVTGCPFDVP RISTKDKKAY KCTLCSDRVA VGQEPACVKT
     CPTGAIMFGT KDAMKDQAAE RIEDLKSRGF EKAGLYDPLG VGGTHVMYVL HHADQPSLYA
     GLPNEPKISP MVSLWKGVAK PLAMFALGAA ALGGLFHFIT KGPNEVSKEL EDEMEREDQK
     AKEA
//
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