ID A0A1Z9F500_9RICK Unreviewed; 913 AA.
AC A0A1Z9F500;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=CBC91_05740 {ECO:0000313|EMBL:OUV76805.1};
OS Rickettsiales bacterium TMED131.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=1986867 {ECO:0000313|EMBL:OUV76805.1, ECO:0000313|Proteomes:UP000196340};
RN [1] {ECO:0000313|EMBL:OUV76805.1, ECO:0000313|Proteomes:UP000196340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED131 {ECO:0000313|EMBL:OUV76805.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000455};
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 -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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:OUV76805.1}.
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DR EMBL; NHGG01000085; OUV76805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9F500; -.
DR Proteomes; UP000196340; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 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; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
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; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 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; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..82
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 183..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 220..275
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 913 AA; 99849 MW; FA878CF00D2152DB CRC64;
MRLVPLRFNG KTIKVDEGVT VLEAARRAGT EVPNVCASDR VGYGPRSSCR LCLVEVAGEH
DLVAACTRRV ERGMAITTRS ARIDQVRRLV AELTLSELTL PGHRSLEGTP FGQLMDRLDV
TETRFGFRTI ESSPDTSHPA VHFMDDACIR CGLCRSACRE AQMNDIILMA GIGSEVHIEF
ESKKPLADTA CTSCGECVQV CPTAALNSYS RTHSHDVRVK RQASTICPYC SVGCRMELQI
TDNKVVTVNG ADGPSNRGRL CVKGRYGLDF LHHPERLTVP LVRKEGAPKD AERQMTSAEI
LELFREASWE EALALAVAGF SEIKDKFGGK HLAVLGSAKN SSEDAYVLQK LARTAFSSPH
VDHCTRLCAS VPPLAEAIGY SAVTAPIEQV FSSDVILMVG SNPEVNHPVA ATFMKNAVRN
GTKLILIDPY DQPFARDATY HLQLRPGTDV ALLSAMTHVI IAEGLFDQSF IEDRLNGYEE
LAKRVAGVSP HTASRICGVP ETLISDAARL FAKAPAAISF WGMGASQHVH GADNIRAVIA
LALICGQIGR PGAGLHPLRG QNNVQGTCDA GLIPSSLPGY RNVLDEEERR FFERAWNSEL
PIGTGLTVVE ILDAAIDGNV KGIYVVGGNP AMANPDLSKT RRALASIEHL VVQDIFPTAT
CAFADVILPA AALPEREGTV TNTDRFVQLL EKSLDAPGNA RPDWEITTAI ASRMGLHWNY
RNVRDIFEEM ARLVPSLTGM SWDLIAKDRS IRYPLDHSSF SNESLFSSAF PTKDGRAHLA
KLNGRGPGEL PDDDYPFVLI TGRVREHWHT GSMTRRSATL DTLSNEPIVY MAPADFTVLG
LEEMDWVSVR TRRGRLKLRA ASDDRLQEGV IWMAMSFFEA AANELTPSSL DDTTHVPEYK
YCAANLESYK NIN
//
