FDXH_HAEIN
ID FDXH_HAEIN Reviewed; 312 AA.
AC P44450;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Formate dehydrogenase iron-sulfur subunit;
DE AltName: Full=Formate dehydrogenase subunit beta;
DE Short=FDH subunit beta;
GN Name=fdxH; OrderedLocusNames=HI_0007;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Allows to use formate as major electron donor during aerobic
CC respiration. The beta chain is an electron transfer unit containing 4
CC cysteine clusters involved in the formation of iron-sulfur centers.
CC Electrons are transferred from the gamma chain to the molybdenum
CC cofactor of the alpha subunit (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AAJ3};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P0AAJ3};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
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DR EMBL; L42023; AAC21685.1; -; Genomic_DNA.
DR PIR; A64042; A64042.
DR RefSeq; NP_438180.1; NC_000907.1.
DR RefSeq; WP_005693893.1; NC_000907.1.
DR AlphaFoldDB; P44450; -.
DR SMR; P44450; -.
DR STRING; 71421.HI_0007; -.
DR EnsemblBacteria; AAC21685; AAC21685; HI_0007.
DR KEGG; hin:HI_0007; -.
DR PATRIC; fig|71421.8.peg.7; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_0_3_6; -.
DR OMA; FCVDRIQ; -.
DR PhylomeDB; P44450; -.
DR BioCyc; HINF71421:G1GJ1-7-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.20.5.480; -; 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 Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF09163; Form-deh_trans; 1.
DR PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR TIGRFAMs; TIGR01582; FDH-beta; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane; Transport.
FT CHAIN 1..312
FT /note="Formate dehydrogenase iron-sulfur subunit"
FT /id="PRO_0000159252"
FT DOMAIN 35..65
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 97..129
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 130..159
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 164..195
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 185
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
SQ SEQUENCE 312 AA; 34069 MW; AA49DD3C17064866 CRC64;
MAGTAQGVQT QDVIKISATS GLTPAPQARD HKVEIAKLID VSTCIGCKAC QVGCSEWNDI
RSDINAQCVG VYDNPVDLDA KAWTVMRFNE VEENDRLEWL IRKDGCMHCT EPGCLKACPA
PGAIIQYANG IVDFQSDKCI GCGYCIAGCP FNIPRMNPED NRVYKCTLCV DRVSVGQEPA
CVKTCPTGAI RFGSKEEMKI YAEQRVADLK SRGYENAGLY DPPGVGGTHV MYVLHHADKP
ELYNGLPKDP QIDLSVTLWK DVLKPVAAVA MGGLALAEVA HYLTVGPNVE EDVEDHHHEF
EENKPSKGEN NE
