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Database: UniProt
Entry: Q2FEI5
LinkDB: Q2FEI5
Original site: Q2FEI5 
ID   FDHL_STAA3              Reviewed;         984 AA.
AC   Q2FEI5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   05-DEC-2018, entry version 91.
DE   RecName: Full=Putative formate dehydrogenase SAUSA300_2258;
DE            EC=1.17.1.9;
GN   OrderedLocusNames=SAUSA300_2258;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
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   -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC       molybdopterin-containing oxidoreductase family. {ECO:0000305}.
DR   EMBL; CP000255; ABD21959.1; -; Genomic_DNA.
DR   RefSeq; WP_001155264.1; NZ_CP027476.1.
DR   ProteinModelPortal; Q2FEI5; -.
DR   SMR; Q2FEI5; -.
DR   PRIDE; Q2FEI5; -.
DR   EnsemblBacteria; ABD21959; ABD21959; SAUSA300_2258.
DR   KEGG; saa:SAUSA300_2258; -.
DR   HOGENOM; HOG000031440; -.
DR   KO; K00123; -.
DR   OMA; TNTAECH; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006478; Formate_DH_asu.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR01591; Fdh-alpha; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; NAD; Oxidoreductase; Repeat.
FT   CHAIN         1    984       Putative formate dehydrogenase
FT                                SAUSA300_2258.
FT                                /FTId=PRO_0000304135.
FT   DOMAIN        3     79       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN       79    119       4Fe-4S His(Cys)3-ligated-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   DOMAIN      138    165       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      181    211       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      257    313       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT   REGION      252    984       Formate dehydrogenase.
FT   METAL        37     37       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        51     51       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        63     63       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        95     95       Iron-sulfur 2 (4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01184}.
FT   METAL        99     99       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       102    102       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       109    109       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       147    147       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       150    150       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       153    153       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       157    157       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       190    190       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       193    193       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       196    196       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       200    200       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       264    264       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       267    267       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       271    271       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
FT   METAL       299    299       Iron-sulfur 5 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   984 AA;  111244 MW;  9EE43448C906B8DE CRC64;
     MQEHLVVTLD GKDYLVEPGT NLLEFIKSQD TFVPSICYNE SMGPIQTCDT CTVEIDGKIE
     RSCSTVIDRP MTVNTVNNDV KDAQKEALDR ILEKHMLYCT VCDYNNGDCE IHNTMDAWGL
     QHQTYEYKEK PYEKDYGPFY RYDPNQCILC GRCVEACQDI EVNETIRIDW DREHPRVIWD
     NDVPINESSC VSCGQCATVC PCNAMMEVNM EGNAGYMTDT EPGSLAAMID LTKKAEPGYG
     PLFAISDSEA EMRKERIKKT KTVCTYCGVG CSFEVWTKDR EILKVQPSHD SPANKIATCV
     KGKFSWGHIN SDQRLTKPLV RKNGEFHEVE WDEALNVIAD NFTAIKEKHG PDALSFISSS
     KATNEESYLM QKLARQVIGT NNVDNCSRYC QAPATKGLFR TVGHGGDSGS IEDLEKAAMS
     VLIGTNTAEA HPVIASRMKR AQKLFGQKIH VFDIRKHEMA ERADRFYQPK PGTDLAWLSA
     VTKYIIDHDL HDKAFIDEWV DDFDEYYKSL ETFTMAFAEE ATGIPESELI KFAEECAKAE
     SVVICWAMGI TQQDIGSDSS TAISNLLLVT GNYRRPGTGA YPLRGHNNVQ GCSDMGSMPD
     KITGYQSIEA DDIRAKFEKE YGVKLNPKAG KDNHEMVEGI HDGEVHSLYL YGEDTGIVDS
     NINFVQAAFE KLDFMVVQDE FLTFTATYAD VVLPASPSLE KDGTFTNTER RIQRLYQALE
     PLGDSKPDWK IFQAIANRLG FDWNYKHPSE IMDEVARLTP LYAGVSYDRL EGFNSLQWPV
     QPDGTDEPIL YLEGFNFDNG KAKLFPLSFD NYFKQDEIYD IHVNNGRLLE HFHEGNMTYQ
     TPMIKYKVPR AFVEISPELA EDRGIHEGAE VKLISETGEA VLQVHVTDRV KGKEIYIPLN
     NDAMENGDLG AINLLTNSDV DQYTDTPSYK RTSCRLEVIT KRGKSPLNPN NFRVNKKRQP
     QYSVQVQKKW ERSDYVFPGN QVDK
//
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