Legends: 1, Iron-sulfur (4Fe-4S). {ECO:0000255|PROSITE-ProRule:PRU01004}; 2, NON_STD Selenocysteine. {ECO:0000305}; 3, SIGNAL Tat-type signal. {ECO:0000255|PROSITE- ProRule:PRU00648}; 4, 4Fe-4S Mo/W bis-MGD-type. {ECO:0000255|PROSITE-ProRule:PRU01004}; 5, ipfam:Molybdop_Fe4S4 [T]; 6, ipat:MOLYBDOPTERIN_PROK_1 [T]; 7, iprf:TAT [T]; 8, iprf:4FE4S_MOW_BIS_MGD [T]; 9, ismart:Molybdop_Fe4S4 [T]; 10, ipat:MOLYBDOPTERIN_PROK_3 [T]; 11, ipfam:Molydop_binding [T].
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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 07-SEP-2016, entry version 113.
DE RecName: Full=Formate dehydrogenase major subunit;
DE EC=1.2.1.2;
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.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA 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
CC site.
CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
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)
CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed
CC by subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of
CC the signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC {ECO:0000255|PROSITE-ProRule:PRU01004}.
DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR OMA; PLHWGFE; -.
DR Proteomes; UP000000579; Chromosome.
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 carrier activity; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR InterPro; IPR009010; Asp_de-COase-like_dom.
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; 2.
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; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; NAD; Oxidoreductase; Periplasm; Reference proteome;
KW Selenocysteine; Signal.
FT SIGNAL 1 33 Tat-type signal. {ECO:0000255|PROSITE-
FT ProRule:PRU00648}.
FT CHAIN 34 1028 Formate dehydrogenase major subunit.
FT /FTId=PRO_0000063224.
FT DOMAIN 43 114 4Fe-4S Mo/W bis-MGD-type.
FT {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT METAL 50 50 Iron-sulfur (4Fe-4S).
FT {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT METAL 53 53 Iron-sulfur (4Fe-4S).
FT {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT METAL 57 57 Iron-sulfur (4Fe-4S).
FT {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT METAL 100 100 Iron-sulfur (4Fe-4S).
FT {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT NON_STD 204 204 Selenocysteine. {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 47 112 ipfam:Molybdop_Fe4S4 [T]
FT MYHIT 48 66 ipat:MOLYBDOPTERIN_PROK_1 [T]
FT MYHIT 1 33 iprf:TAT [T]
FT MYHIT 43 114 iprf:4FE4S_MOW_BIS_MGD [T]
FT MYHIT 43 112 ismart:Molybdop_Fe4S4 [T]
FT MYHIT 934 961 ipat:MOLYBDOPTERIN_PROK_3 [T]
FT MYHIT 117 591 ipfam:Molybdopterin [T]
FT MYHIT 898 1018 ipfam:Molydop_binding [T]
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
//
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