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Database: UniProt
Entry: A0A412L6J8_9FIRM
LinkDB: A0A412L6J8_9FIRM
Original site: A0A412L6J8_9FIRM 
ID   A0A412L6J8_9FIRM        Unreviewed;       655 AA.
AC   A0A412L6J8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:RGS76616.1};
DE   Flags: Fragment;
GN   ORFNames=DWX73_11810 {ECO:0000313|EMBL:RGS76616.1};
OS   Coprococcus sp. AF21-14LB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=2292231 {ECO:0000313|EMBL:RGS76616.1, ECO:0000313|Proteomes:UP000285019};
RN   [1] {ECO:0000313|EMBL:RGS76616.1, ECO:0000313|Proteomes:UP000285019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF21-14LB {ECO:0000313|EMBL:RGS76616.1,
RC   ECO:0000313|Proteomes:UP000285019};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGS76616.1}.
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DR   EMBL; QRVX01000064; RGS76616.1; -; Genomic_DNA.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000285019; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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.
PE   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000285019};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Selenium {ECO:0000313|EMBL:RGS76616.1};
KW   Selenocysteine {ECO:0000313|EMBL:RGS76616.1}.
FT   DOMAIN          1..78
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          78..117
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          139..172
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          182..211
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          219..274
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   NON_STD         354
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000313|EMBL:RGS76616.1"
FT   NON_TER         655
FT                   /evidence="ECO:0000313|EMBL:RGS76616.1"
SQ   SEQUENCE   655 AA;  71625 MW;  DD58BEE5E4A0280A CRC64;
     MINVTINGME IQAKEGQTIL KAARENGIHI PTLCFLEGIN EIGSCRICVV EIEGRAGLAT
     ACNTVVREGM KIQTDSEAVV EARKNTLHLL MAEHKTNCFK CIKNGACELQ ALAREYGIDV
     PNFKASHGDV QHEPCAENPF LSYDPGLCIQ CQRCISTCAK ATGRHALSLE KNGARVYVKA
     PFGEGWKESL CESCGNCAQA CPTGALVIKR RKDYRDWEVK KVRTTCPHCA TGCQMDLIVK
     NGKIVDVQGA DGPSNHGLLC VKGRSGSFDF VDCEDRIRYP LIKNKETGEF ERATWDEALD
     LVASKFTEIK KQYGGEALAG FACSRSTNED IYMLQKMVRT AFESNNTDNC ARVUHAPTVA
     GLATTLGSGA MTNTIYDITH ESDAIMLVGS NPEHAHPVLG MQVRQAVQRG AKLIVVDPRD
     IDLCKDADIH LKLKPGTNVA FANGMMHIFI EEDLVDHKFI EERTENFEAM KELVKDYTPE
     KVAEICGIDA DALREAARIY ATANRAPIMY CLGVTEHHTG TEGVMSLSNM AMMVGKIGKP
     GCGVNPIRGQ NNVQGACDMG ASPNQFSGYQ NIDKPGVLEK FEEAWGTKLN PNIGTKATDC
     FPKMLTGEVK GLFIFGEDPV RTDPNTHHVI KALSSLDFFV VDELFMTETA KGTTG
//
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