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Database: UniProt
Entry: A0A0M3AQ22_9SPHN
LinkDB: A0A0M3AQ22_9SPHN
Original site: A0A0M3AQ22_9SPHN 
ID   A0A0M3AQ22_9SPHN        Unreviewed;       765 AA.
AC   A0A0M3AQ22;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KKW90639.1};
GN   ORFNames=YP76_18890 {ECO:0000313|EMBL:KKW90639.1};
OS   Sphingobium chungbukense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW90639.1, ECO:0000313|Proteomes:UP000033874};
RN   [1] {ECO:0000313|EMBL:KKW90639.1, ECO:0000313|Proteomes:UP000033874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ77 {ECO:0000313|EMBL:KKW90639.1,
RC   ECO:0000313|Proteomes:UP000033874};
RA   Kim Y.-C., Chae J.-C.;
RT   "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT   chungbukense DJ77.";
RL   Submitted (APR-2015) 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=[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:KKW90639.1}.
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DR   EMBL; LBIC01000009; KKW90639.1; -; Genomic_DNA.
DR   RefSeq; WP_046765139.1; NZ_LBIC01000009.1.
DR   AlphaFoldDB; A0A0M3AQ22; -.
DR   STRING; 56193.YP76_18890; -.
DR   PATRIC; fig|56193.3.peg.3973; -.
DR   Proteomes; UP000033874; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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}.
FT   DOMAIN          111..489
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          646..754
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   765 AA;  84473 MW;  201141E5014A4ED9 CRC64;
     MDKPEDETVH YDGPAGGWGS LKGISRIYAK ELASPAVIET LRRQNKPGGF MCVSCAWTKP
     AHPHPAEFCE NGAKATLWEL TSRRCTPEFF DRHSVSELKE WPDHDLEQEG RLTHPMRYDR
     ASDRYLPVSW AEAFREIGAE LRALDPKSTA FYTSGRASLE TSYLYALFAR LYGHNNLPDS
     SNMCHETTSV GLKKVTGSPV GTCVLSDFDQ CDAIFFFGQN TGSNSPRFLH PLQEAVKRGC
     RIVTFNPVQE PGLIKFVNPQ SPTEMLTKKS TPISELYFQV RPGGDIAAIM GLCKHVLARD
     AELFARDKRH LIDTAFIEQH CHGYDDFVAC ANAASWEEIE RESGLSRADL EAAADIYCDA
     EKVIGIYGMG VTQHVHGSQT IGMLVNLLLL RGNIGREGAG ISPVRGHSNV QGQRTVGISE
     KPELVPNDRL KRLFDFEPPM DKGMNTVEAC EGIIAGKVKA FVSLGGNFVR AIPERGKMEG
     AWTKMHLTVQ IATKLNRSHL INGEIAYLLP CLGRSEEDMQ ASGPQTVTME DSLSCIHGSV
     GKRKPASEHL LSELAIVTGI AKETLPPNPK VRWDEWVGDY GKVRDLIEAS YPDKFTDFND
     RLFTPGGFYK GSKARERIWK AESGKAEFTV PTTLSSCGFD DAPGRYRLIT LRSNDQFNTT
     IYGYSDRMRG IEGTRDVLLI NPDEMARAGL AAGQVVALVS DAEDGVHREV GGLTVTPFSL
     PDRCVAAYYP EMNPLVPLSH HDKLSKTPAA KSVPVRIRAN DCSSR
//
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