(data stored in SCRATCH zone)

SWISSPROT: Q13DH8_RHOPS

ID   Q13DH8_RHOPS            Unreviewed;       948 AA.
AC   Q13DH8;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ABE37861.1};
GN   OrderedLocusNames=RPD_0623 {ECO:0000313|EMBL:ABE37861.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37861.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37861.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37861.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000283; ABE37861.1; -; Genomic_DNA.
DR   RefSeq; WP_011501048.1; NC_007958.1.
DR   STRING; 316057.RPD_0623; -.
DR   EnsemblBacteria; ABE37861; ABE37861; RPD_0623.
DR   KEGG; rpd:RPD_0623; -.
DR   eggNOG; ENOG4108IEG; Bacteria.
DR   eggNOG; COG3383; LUCA.
DR   HOGENOM; HOG000031440; -.
DR   KO; K00123; -.
DR   OMA; DGTPTMH; -.
DR   OrthoDB; 323168at2; -.
DR   BioCyc; RPAL316057:RPD_RS03195-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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   CDD; cd02753; MopB_Formate-Dh-H; 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; IPR041924; Formate_Dh-H_N.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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.
PE   4: Predicted;
DR   PRODOM; Q13DH8.
DR   SWISS-2DPAGE; Q13DH8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Iron {ECO:0000256|SAAS:SAAS00454562};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00454505};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00077323};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01133048}.
FT   DOMAIN       18     96       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
FT   DOMAIN       96    135       4Fe-4S His(Cys)3-ligated-type.
FT                                {ECO:0000259|PROSITE:PS51839}.
FT   DOMAIN      158    189       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      201    230       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      237    293       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000259|PROSITE:PS51669}.
SQ   SEQUENCE   948 AA;  103135 MW;  623C1A9A3075A692 CRC64;
     MALVHEIDFG TPRSPSETMV TLTIDGRSVS VPEGTSIMRA AMEIGTAIPK LCATDMVDAF
     GSCRLCLVEI DGRSGTPASC TTPVADGLVV KTQTERLKQI RKGVMELYIS DHPLDCLTCS
     ANGDCELQDM AGAVGLRDVR YGYSGNKHPN PGLDESNPYF TYDASKCIVC SRCVRACEEV
     QGTFALTIAG RGFGSVVSPG MQESFLGSEC VSCGACVQAC PTATLNEKSV IEIGTPERSV
     VTTCAYCGVG CTFKAEMRGE EVVRMVPYKD GKANRGHSCV KGRFAWGYTN HKERILKPMI
     RARITDPWRE VSWDEAFSHA ASELKRIQAK YGRDSIGGIT SSRCTNEETF LVQKLIRAGF
     GNNNVDTCAR VCHSPTGYGL STAFGTSAGT QDFDSVEHTD VVMIIGANPT DGHPVFASRL
     KKRLRAGAKL IVVDPRRIDL VRSAHVEAAQ HLPLKPGTNV AVLTALAHVI VTEGLANEAF
     VRERCDWSEY EHWASFVAQP NNSPEATAAM TGVDPQALRE AARLYATGGN GAIYYGLGVT
     EHSQGSTTVM AIANLAMVTG NLGRQGVGVN PLRGQNNVQG ACDMGSFPHE LPGYRHISTD
     AVRDSFEALW GVTLNSEPGL RIPNMLDAAV DGSFKALYVQ GEDILQSDPN TKHVAAGLEA
     MECVIVHDLF LNETANYAHI FLPGSTFLEK NGTFTNAERR IQRVRKVMTP KNGLEDWEVT
     LRLAEAMGFK MSYDHPSQIM DEIATLTPTF TGVSYARLDE LGSIQWPCNA NAPEGTPVMH
     IDHFVRGKGK FVITEYVATD ERTGPRFPLL LTTGRILSQY NVGAQTRRTA NTVWHDEDRL
     EIHPHDAEQR GVRDGDWVRL ASRAGETTLR ALITDRVAPG VVYTTFHHPD TQANVVTTEY
     SDWATNCPEY KVTAVQVSPS NGPSEWQRAY EEQATAARRI ASAAEAAE
//

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