ID D7CNB2_SYNLT Unreviewed; 1075 AA.
AC D7CNB2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ADI02197.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ADI02197.1};
GN OrderedLocusNames=Slip_1434 {ECO:0000313|EMBL:ADI02197.1};
OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophothermus.
OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI02197.1, ECO:0000313|Proteomes:UP000000378};
RN [1] {ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX DOI=10.4056/sigs.1233249;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1T).";
RL Stand. Genomic Sci. 3:267-275(2010).
RN [2] {ECO:0000313|EMBL:ADI02197.1, ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX PubMed=21304731;
RA Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1).";
RL Stand. Genomic Sci. 3:268-275(2010).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP002048; ADI02197.1; -; Genomic_DNA.
DR STRING; 643648.Slip_1434; -.
DR KEGG; slp:Slip_1434; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_0_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000000378; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer 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: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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADI02197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000378};
KW Selenium {ECO:0000313|EMBL:ADI02197.1};
KW Selenocysteine {ECO:0000313|EMBL:ADI02197.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 43..105
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 210
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADI02197.1"
SQ SEQUENCE 1075 AA; 120067 MW; E0BDC36D8553AFDD CRC64;
MKVTRRQFLK ITGATAATFA VVDLGFNLKV VAAEVKEFRI KDVTPMPTIC PYCASGCGLL
VYSERDASGN YVKLLSVEGD PDNPINRGGA CAKGAALFNL REIYDEATGK QVPNPKRATK
PLYRASKSDK WEEKDWDWIL DEIAKRVKKT RDESFIYKEK LEDGTEIIVS RTEKIGSMGG
SGLDNEECYL LSKLMRALGV VYLETQARIU HSSTVAGLSP SFGRGVMTNH VVDIKNSDCV
LIIGGNTAEN HPIAMKWALK AREERGAKII HVDPRFTRTS AVADIYAPLR SGTDIAFIGG
MIKYALDNEL YSKEYVLNYT NASFIVADTY NFDPETGLFS GYTFDEQKKI GQYDQKMWDY
KRDEKGMPLK DPTLTDPRCV FQLLKQHYSR YDIDTVCRIT GTPKDKYLEV LKTYCATGAV
DKVGTILYAM GTTQHSVGSQ NCRIYAILQL LLGNVGRPGG GVNAMRGENN VQGATDMALL
NHYIPGYVTC PTNTADHKDL LAFLKKETPG AAKVAATNLD EFRAAVAAGI PNSGFRINTS
KWVVSMLKAW WGDAATPDND FAYHYLPKRD AKKNYSHMGM FEAMYNGELD GLFINGGNPI
VGGPNANKEQ IALTKLKWLV VLDLWLHETA EFWSYTAWER PVENDKVPKL KPSDIETEVF
FLPAAGVYEK EGTASNTGRW MQYRWKAADP LGESKPDLWI INELAKRIKK LYEGSTKPQD
EPITKLVWGP YGEGEEPEPI KVGLELNGYT VADGKPVENF TKLADDGSTA CGCWVYSGCM
TTKEDGSLDY KPMWRNNTDN SKTGLGLFSK WSWSWPLNRR IVYNRCSIRP DGTPWPGDEA
RALFKWDPNA PGDPKKPGTM GMWVGDDVPD FNKYLAPTTE PCAAIPYLMR PEGVACLYST
NGMKDGPFPE HYEPWESPVT KNLLNGSQFN PVAKAWDPDK RGVADKFPII GTTYRVTEHW
QTGALTRNLP WLAELMPNMF VEISEELARL KGIKNGDKVI VSTTRGDIKA VAFVTKRLKP
FIIDGKEVHQ IGMTWHYGFK GYAKGDPANR LTPHVGDPNS MIPEYKAWLC DVRRA
//
