ID A0A0Q5V6J2_9SPHN Unreviewed; 762 AA.
AC A0A0Q5V6J2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KQS51810.1};
GN ORFNames=ASG20_02940 {ECO:0000313|EMBL:KQS51810.1};
OS Sphingomonas sp. Leaf198.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS51810.1, ECO:0000313|Proteomes:UP000050871};
RN [1] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Garrido-Oter R.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS51810.1}.
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DR EMBL; LMPX01000001; KQS51810.1; -; Genomic_DNA.
DR RefSeq; WP_056050344.1; NZ_LMPX01000001.1.
DR AlphaFoldDB; A0A0Q5V6J2; -.
DR STRING; 1736299.ASG20_02940; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000050871; Unassembled WGS sequence.
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 CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 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; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050871}.
FT DOMAIN 112..413
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
SQ SEQUENCE 762 AA; 83723 MW; FB1214FA7ABE8CAA CRC64;
MSDDRTVEIE DYTAPAGGWG SMKSLVEISA REKVGPEVIR ELARQNKPDG FACVSCAWGK
PAHPHVAEFC ENGAKATAWE LTSFRVTPAF FEQHTVSELI GWKDYDLEQA GRLTHPLKYD
ANTDKYAACS WDEAFAGIGA KLKTYDPTKV IFYASGRASL ETSYMYSLLA RMYGSQNLPD
SSNMCHETTS VGLKSAIGSA VGTIHLSDYE KCDAIFYFGQ NPGVNSPRFL HPLRDCAKRG
VEIVVFNPLK ERGLEKFQDP QNPIEMVTGK STPIASQYHQ LKTGGDVGAI MGMCKYLIEA
DDNAKRINGL PVLDHAFLAE HTTGFEAFAE VARATEWATI EHESGLPRTE IEAAAKVYAK
SKAVIAVYGM GLTQHVGGID NVHMVVNLML LRGNIGKPGA GMGPVRGHSN VQGQRTVGIT
EKPELAPLDK LAEQYGFEPP REKGWDTVEA CEAVLDGSAQ AFVGLGGNFV RAIPDHARME
PKWRALDLTV HIATKLNRSH LLPGETSYLL PCLGRIETDM QGTGPQSVSI EDSFSQIYGS
KGKATPASET LLSEPAIVAG IAKATLAPNP KLDWDAWVRD YARVRDAIEV TYPDLFKNFN
DQMFTPGGFW KGVPAAHREW KTKSGKAEIN VPQALNVTGF EEAEGRFRLM TLRSNDQFNT
TVYGYHDRFR GVKGTRDIVF MNRSDMIRMG ITDGDDVDLV GDAGDNSDRR LNKLRVVEYA
IPEGCLGAYY PESNLLIPVA HHARESHVPA AKSVPVRIEK TR
//