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Database: UniProt
Entry: A0A220W707_9SPHN
LinkDB: A0A220W707_9SPHN
Original site: A0A220W707_9SPHN 
ID   A0A220W707_9SPHN        Unreviewed;       712 AA.
AC   A0A220W707;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:ASK88604.1};
DE            EC=1.17.99.7 {ECO:0000313|EMBL:ASK88604.1};
GN   Name=fdhF {ECO:0000313|EMBL:ASK88604.1};
GN   ORFNames=SPHFLASMR4Y_01858 {ECO:0000313|EMBL:ASK88604.1};
OS   Sphingorhabdus sp. SMR4y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2584094 {ECO:0000313|EMBL:ASK88604.1, ECO:0000313|Proteomes:UP000198359};
RN   [1] {ECO:0000313|EMBL:ASK88604.1, ECO:0000313|Proteomes:UP000198359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMR4y {ECO:0000313|EMBL:ASK88604.1,
RC   ECO:0000313|Proteomes:UP000198359};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated from a
RT   culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP022336; ASK88604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220W707; -.
DR   KEGG; sfla:SPHFLASMR4Y_01858; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000198359; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02775; MopB_CT; 1.
DR   Gene3D; 2.40.40.20; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:ASK88604.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198359}.
FT   DOMAIN          3..59
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   712 AA;  76906 MW;  F71D63951B96D140 CRC64;
     MAVETKRSFC RFCHASCAMI VEVEDDKVKS VRGDKEDHLF HGYTCIKGRQ LPDMHNLPDR
     MITSKIRQPD GSFRDISTAE ALKLAGEQMK KMVEEHGPHS IAVYCGTNAF QNSAVLGTSY
     AFAQGIGSRN WYTSVTVDQP AKVFTTARYG MWMGGGNAFT ESDVAMFVGN NPIVSHYSGG
     MPTSSPSRGL RDAKARGLKV IVADPRVSEM GKLADIYLPV KPGEDPALLA GMLNVIFEEK
     LYDQNFVAAH VDGVEELEAA VKHMTPDIAA KRAGVEKDQL VAAARMFAGA NKGRVVTGTG
     PEMAGNGTLT EYLVASLNIL CARFNQEGER VSAPMVFNPL MGGPKKAQVA PKMPTFGEGF
     PKSRIRGLGH LGKEMPCNVL ADEILTPGDG QVRALISIGG NPEIAFPDQQ KVRRALDECE
     LFIQIDPWMS ASARRADMIL APSMCLERED INNVSDAFTE EAYGHYTEAM VPPPGDTMDE
     YEMLWWLAKH MGIEMNFPGG PVSMETCPDK ATVLDLISEG SLLKPSKAKA DAAALERKGA
     AITYDELHPV VGPADPDAQE KFDLNAGAMP SELIDYAAND PVESGFDFRL ISRRSKHRYN
     SNGHTFPKLV EKMPTNPAFF NPADLAAAGI EDGAIIEISS PTASIFGLAK ADDKVRPGVI
     SMSHAFGDSE AGKDDVMTKG GSTNRLIVDN DHIDPITGQA MQSAIPVKIA AA
//
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