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Database: UniProt
Entry: Q2YYT1
LinkDB: Q2YYT1
Original site: Q2YYT1 
ID   FDHL_STAAB              Reviewed;         984 AA.
AC   Q2YYT1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-DEC-2018, entry version 95.
DE   RecName: Full=Putative formate dehydrogenase SAB2186c;
DE            EC=1.17.1.9;
GN   OrderedLocusNames=SAB2186c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81875.1; -; Genomic_DNA.
DR   RefSeq; WP_001155290.1; NC_007622.1.
DR   ProteinModelPortal; Q2YYT1; -.
DR   SMR; Q2YYT1; -.
DR   EnsemblBacteria; CAI81875; CAI81875; SAB2186c.
DR   KEGG; sab:SAB2186c; -.
DR   HOGENOM; HOG000031440; -.
DR   KO; K00123; -.
DR   OMA; TNTAECH; -.
DR   BioCyc; SAUR273036:G1G1D-2436-MONOMER; -.
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; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW   Oxidoreductase; Repeat.
FT   CHAIN         1    984       Putative formate dehydrogenase SAB2186c.
FT                                /FTId=PRO_0000304128.
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;  111309 MW;  D9148E8BB9B4DA02 CRC64;
     MQEHLVVTLD GKDYLVEPGT NLLEFIKSQD TFVPSICYNE SMGPIQTCDT CTVEIDGKIE
     RSCSTVIDRP MTVNTVNNDV KDAQKEALDR ILEKHMLYCT VCDYNNGDCE IHNTMDAWGL
     QHQTYEYKEK PYEKDYGPFY RYDPNQCILC GRCVEACQDI EVNETIRIDW DREHPRVIWD
     NDVPINESSC VSCGQCATVC PCNAMMEVNM EGNAGYMTDT EPGSLAAMVD LTKKAEPGYG
     PLFAISDSEA EMRKERIKKT KTVCTYCGVG CSFEVWTKDR EILKVQPSHD SPANKIATCV
     KGKFSWGHIN SDQRLTKPLV RKNGEFHEVE WDEALNVIAD NFTSIKEKYG PDALSFISSS
     KATNEESYLM QKLARQVIGT NNVDNCSRYC QAPATKGLFR TVGHGGDSGS IEDLEKAAMS
     VLIGTNTAEA HPVIASRMKR AQKLFGQKIH VFDIRKHEMA ERADRFYQPK PGTDLAWLSA
     VTKYIIDHDL HDKAFIEEWV EDFDEYYKSL ETFTMAFAEE ATGIPEAELI KFAEECAKAE
     SVVICWAMGI TQQDIGSDSS TAISNLLLVT GNYRRPSTGA YPLRGHNNVQ GCSDMGSMPD
     KITGYQSIEA DDIRAKFEKE YGVKLNPKVG KDNHEMVEGV HDGEIHSLYL YGEDTGIVDS
     NINFVQAAFE NLDFMVVQDE FLTFTATFAD VVLPASPSLE KDGTFTNTER RIQRLYQALK
     PLGESKPDWK IFQAIANKLG FDWNYKHPSE IMDEIARLTP LYAGVSYERL EGFNSLQWPV
     HPDGTDEPIL YLEGFNFDNG KAKLFPLSFD NYFKQDEVYD IHVNNGRLLE HFHEGNMTYQ
     TPMIKYKVPR AFVEISPELA EDRGIHEGAE VKLISETGEA VLQVHVTDRV KGKEIYIPLN
     NDAMENGDLG AINLLTNSDV DQYTDTPSYK RTSCRLEVIA KRGKSPLNPN NFRVNKKRHP
     QYSVQVQKKW ERPDYVFPGN QVDK
//
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