FDXI_HAEIN
ID FDXI_HAEIN Reviewed; 238 AA.
AC P44451;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Formate dehydrogenase, cytochrome b556 subunit;
DE AltName: Full=Formate dehydrogenase subunit gamma;
DE Short=FDH subunit gamma;
GN Name=fdxI; OrderedLocusNames=HI_0008;
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).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allows to use formate as major electron donor during
CC anaerobic respiration. Subunit gamma is probably the cytochrome
CC b556(FDO) component of the formate dehydrogenase (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. Heme 1 is located at the
CC cytoplasmic interface, heme 2 is located at the periplasmic interface.
CC Electrons are transferred from the periplasmic to the cytoplasmic heme.
CC {ECO:0000250};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21686.1; -; Genomic_DNA.
DR RefSeq; NP_438181.1; NC_000907.1.
DR RefSeq; WP_005663315.1; NC_000907.1.
DR AlphaFoldDB; P44451; -.
DR SMR; P44451; -.
DR STRING; 71421.HI_0008; -.
DR EnsemblBacteria; AAC21686; AAC21686; HI_0008.
DR KEGG; hin:HI_0008; -.
DR PATRIC; fig|71421.8.peg.8; -.
DR eggNOG; COG2864; Bacteria.
DR HOGENOM; CLU_091368_1_1_6; -.
DR OMA; TIMSMIF; -.
DR PhylomeDB; P44451; -.
DR BioCyc; HINF71421:G1GJ1-8-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR GO; GO:0015944; P:formate oxidation; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR InterPro; IPR006471; Formate_DH_gsu.
DR Pfam; PF01292; Ni_hydr_CYTB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR TIGRFAMs; TIGR01583; formate-DH-gamm; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="Formate dehydrogenase, cytochrome b556 subunit"
FT /id="PRO_0000087217"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 238 AA; 27758 MW; 4D0744AA342066A2 CRC64;
MSKIEISNDT RIIRHRTPAR ISHWMLVICF FMTMFTGVAF FFPDFAWLTE ILGTPQIARA
IHPFTGILMF FAFIYLALLY WDHNIPEKND IRWAKGVIEV LKGNEHAVAD NGKYNLGQKM
LFWTLNLAMV TLLVTGIIMW RQYFSHYFSI PVLRIAILLH SASAFMLFTG ILVHIYMAFW
VKGSIRGIVE GWVTVRWAKK HHPRWYREEV LSKLEEDLLN EQSGKVGKTK VLFKGFGK
