ID R8ARJ1_PLESH Unreviewed; 803 AA.
AC R8ARJ1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Formate dehydrogenase-O major subunit {ECO:0000313|EMBL:EON88955.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:EON88955.1};
GN ORFNames=PLESHI_07405 {ECO:0000313|EMBL:EON88955.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON88955.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON88955.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON88955.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:EON88955.1}.
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DR EMBL; AQQO01000047; EON88955.1; -; Genomic_DNA.
DR AlphaFoldDB; R8ARJ1; -.
DR PATRIC; fig|1315976.3.peg.1455; -.
DR HOGENOM; CLU_000422_1_2_6; -.
DR Proteomes; UP000014012; Unassembled WGS sequence.
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: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; 3.40.50.740; -; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF6; FORMATE DEHYDROGENASE-O MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EON88955.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT DOMAIN 2..443
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 678..796
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 803 AA; 89261 MW; 8A4614088D9DF7FA CRC64;
MTNHWVDIKN ANLIVVMGGN AAEAHPVGFR WAMEAKIHNN AKIIVIDPRF TRTASVADFY
TPIRSGTDIA FLSGVILYLM NNHKINQEYV NAYTNASLLV RPDFGFEDGL FTGYDAEKRK
YDKSTWAYQL DENGFAKRDP SLQDPQCVWN LLKQHVSRYT PEVVSNLCGT PKEDFLTVCQ
LIAETSAKDK TASFLYALGW TQHSIGAQNI RTMAMIQLLL GNMGMAGGGI NALRGHSNIQ
GLTDLGLLSQ SLPGYLTLPS EKQPDLQTYL TAMTPKPLLE GQVNYWGNYP KFFVSLMKSF
YGDKAQPENS WGYDWLPKWD KGYDVLQYFE MMSQGKVNGY LCQGFNPVAS FPNKNKVVAS
LSKLKYLVII DPLNTETANF WQNHGEFNDV NPADIQTEVF RLPSTCFAEE NGSIVNSGRW
LQWHWKGADA PGEALGDGEI LAGLFSTLRE LYANEGGALP EQVLNMSWNY LQPHNPQAEE
VAMENNGKAL ADLRDADGNV IVKKGQQLSS FAQLRDDGST SSGCWIFAGS WTPEGNQMAR
RDNADPSGLG NTLGWAWAWP LNRRILYNRA SADPAGKPWD PKRKLISWND GKWTGIDIAD
YSTAAPDSGV GPFIMQPEGL GRLFALDKMA EGPFPEHYEP FETPLGTNPL HPNVVSNPAA
RVFKDDLAAM GSAKEFPFVA TTYRLTEHFH YWTKHARLNA IIQPEQFIEI GETLAAKKGI
QHGDTVKVSS NRGYIKAKAV VTKRIRTLQV NGQEVDTIGI PIHWGFEGVA KKGFLANTLT
PFVGDANTQT PEFKAFLVNV EKV
//
