ID   A0A1R4A4B1_HALED        Unreviewed;       759 AA.
AC   A0A1R4A4B1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Probable molybdopterin-dependent oxidoreductase YdeP {ECO:0000313|EMBL:SJK83801.1};
GN   Name=ydeP {ECO:0000313|EMBL:SJK83801.1};
GN   ORFNames=HELO_2482D {ECO:0000313|EMBL:SJK83801.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:SJK83801.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
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}.
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DR   EMBL; FN869568; SJK83801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4A4B1; -.
DR   KEGG; hel:HELO_2482D; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000008707; Chromosome.
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; 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; 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          113..486
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          641..747
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   759 AA;  83913 MW;  DB1FA0E593856AA9 CRC64;
     MVGKRKIPGI KNYRGPAGGW GALKATATAV REQMETIKPP LTLLRTNQPD GFDCPGCAWP
     DKEHRSTFQF CENGAKAVTW EATSKRVRPD FFESHTVTSL LEYSDYELEN LGRLTHPLAY
     DKETDTFRAI EWQDAFHRIG EILRKLPPDA VEFYTSGRAS NEAAFLYQLF AREYGTNNFP
     DCSNMCHEAT SVGLPRSIGI GKGTVSLDDF DECELIIAIG HNPGTNHPRM MGTLHEASRR
     KVPIMVFNPL RERALERFAD PQNMIEMATY GSTRIASSYF QVKAGGDAAA IKGIMKSLLE
     MEESVGDVLD HDFINRHTVG FDELVDDLAA TKWSDIEAVS GIGRSDLEMV AAAYAKSSAT
     IVSYGMGVTQ HNQGTANVRL ICDLLMLRGN FGKPGAGICP LRGHSNVQGN RTVGITERPD
     ASFLENLEHV FGFEAPKKQG HDAVQAMQSM VRRDSKALFC LGGNFAVALP DPAQSYQAMR
     ALDLSVHVAT KLNRSHLLVG KETYLFPCLG RTEQDIQRSG PQSVTVEDSM SMVHASAGKL
     QPASEHLKSE PAIVAGIAAN ALPESNVPWN DLVADYDNIR DLIEKTIPGF DDYNDRIRVP
     GGFRMPLPPT ERKWETPSGK AEFYVFDGLR ADKKVHGDDV LRLVTIRSHD QYNTTIYAMD
     DRYRGVFGRR DVLFMSKSDL QDRGLQQGDL VNIETVSDGE ALHYDGLTAI EYSIAPGTIA
     AYYPEANRLV PLDYIDKDSG TPSYKSIPVR VRRAGESPA
//