Entry sw: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   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        43    114       iprf:4FE4S_MOW_BIS_MGD [T]
FT   MYHIT       117    591       ipfam:Molybdopterin [T]
FT   MYHIT         1     33       iprf:TAT [T]
FT   MYHIT        48     66       ipat:MOLYBDOPTERIN_PROK_1 [T]
FT   MYHIT        47    112       ipfam:Molybdop_Fe4S4 [T]
FT   MYHIT       898   1018       ipfam:Molydop_binding [T]
FT   MYHIT       934    961       ipat:MOLYBDOPTERIN_PROK_3 [T]
FT   MYHIT        43    112       ismart:Molybdop_Fe4S4 [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
//