FDXG_HAEIN
ID FDXG_HAEIN Reviewed; 1028 AA.
AC P46448;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Formate dehydrogenase major subunit;
DE EC=1.17.1.9;
DE AltName: Full=Formate dehydrogenase subunit alpha;
DE Short=FDH subunit alpha;
DE Flags: Precursor;
GN Name=fdxG; OrderedLocusNames=HI_0006;
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
CC anaerobic respiration. Subunit alpha possibly forms the active site.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PRIDE; P46448; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01553; formate-DH-alph; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase;
KW Periplasm; Reference proteome; Selenocysteine; Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..1028
FT /note="Formate dehydrogenase major subunit"
FT /id="PRO_0000063224"
FT DOMAIN 43..114
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT NON_STD 204
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1028 AA; 115451 MW; 4A2E55B78B301300 CRC64;
MQVSRRKFFK ICAGGMAGTS AAMLGFAPAN VLAAPREYKL LRAFESRNTC TYCAVSCGML
LYSTGKPYNS LSSHTGTNTR SKLFHIEGDP DHPVSRGALC PKGAGSLDYV NSESRSLYPQ
YRAPGSDKWE RISWKDAIKR IARLMKDDRD ANFVEKDSNG KTVNRWATTG IMTASAMSNE
AALLTQKWIR MLGMVPVCNQ ANTUHGPTVA SLAPSFGRGA MTNNWVDIKN ANLIIVQGGN
PAEAHPVGFR WAIEAKKNGA KIIVIDPRFN RTASVADLHA PIRSGSDITF LMGVIRYLLE
TNQIQHEYVK HYTNASFLID EGFKFEDGLF VGYNEEKRNY DKSKWNYQFD ENGHAKRDMT
LQHPRCVINI LKEHVSRYTP EMVERITGVK QKLFLQICEE IGKTSVPNKT MTHLYALGFT
EHSIGTQNIR SMAIIQLLLG NMGMPGGGIN ALRGHSNVQG TTDMGLLPMS LPGYMRLPND
KDTSYDQYIN AITPKDIVPN QVNYYRHTSK FFVSMMKTFY GDNATKENGW GFDFLPKADR
LYDPITHVKL MNEGKLHGWI LQGFNVLNSL PNKNKTLSGM SKLKYLVVMD PLQTESSEFW
RNFGESNNVN PAEIQTEVFR LPTTCFAEEE GSIVNSGRWT QWHWKGCDQP GEALPDVDIL
SMLREEMHEL YKKEGGQGIE SFEAMTWNYA QPHSPSAVEL AKELNGYALE DLYDPNGNLM
YKKGQLLNGF AHLRDDGTTT SGNWLYVGQW TEKGNQTANR DNSDPSGLGC TIGWGFAWPA
NRRVLYSRAS LDINGNPWDK NRQLIKWNGK NWNWFDIADY GTQPPGSDTG PFIMSAEGVG
RLFAVDKIAN GPMPEHYEPV ESPIDTNPFH PNVVTDPTLR IYKEDREFIG SNKEYPFVAT
TYRLTEHFHS WTAQSALNII AQPQQFVEIG EKLAAEKGIQ KGDMVKITSR RGYIKAVAVV
TKRLKDLEID GRVVHHIGLP IHWNMKALNG KGNRGFSTNT LTPSWGEAIT QTPEYKTFLV
NIEKVGEA
