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Database: UniProt
Entry: A4XZN1_PSEMY
LinkDB: A4XZN1_PSEMY
Original site: A4XZN1_PSEMY 
ID   A4XZN1_PSEMY            Unreviewed;       770 AA.
AC   A4XZN1;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Oxidoreductase alpha (Molybdopterin) subunit {ECO:0000313|EMBL:ABP86797.1};
GN   OrderedLocusNames=Pmen_4050 {ECO:0000313|EMBL:ABP86797.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP86797.1};
RN   [1] {ECO:0000313|EMBL:ABP86797.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ymp {ECO:0000313|EMBL:ABP86797.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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}.
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DR   EMBL; CP000680; ABP86797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XZN1; -.
DR   STRING; 399739.Pmen_4050; -.
DR   KEGG; pmy:Pmen_4050; -.
DR   PATRIC; fig|399739.8.peg.4101; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_6; -.
DR   OrthoDB; 5287431at2; -.
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          109..561
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          649..736
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   770 AA;  84620 MW;  CB767E6F7A8E2DD5 CRC64;
     MKPRFKPYRG PSGGWGSAYS VGSILLRERA PLTGAMALLK QNRPISGFAC VSCAWAKPHP
     SKPLAFCENG AKATAWETTS LRCTPEFFAQ HRLSELRNWS DYDLEQQGRL THPMRWDATS
     DRYLPVSWDQ AIAEIGAELK ALDDPDQAVF YASGRASLEA SYLWQLLARR FGTNNLPDSS
     NMCHESTSVA LPESIGVPVG TVTLNDFAKT DGILIFGHNT SSNSPRLLHD LEAARGRDAP
     ILTFNPLRER GLERFTDPQS PTQMLSGHSI VVSTHYHQVA IGGDVAAIAG ICKALLALDD
     EALASGQPSV LDRVFIEQHT QGFEAFEQAV RAYAWADLER RSGLTRGAME GAAKVYAGCQ
     RVIAIYGMGL TQHRHGVTNI QMLVNLLLMR GNLGKEGAGI CPVRGHSNVQ GQRTVGITEQ
     VAQVPVERLR EQFAFEVPAE DGVSTVDACE GIIAGRIRAF LSLGGNFVRA APDSHRLEPA
     WSKLRLTVQI VTKLNRSALV HGEKAYILPC LGRTEMDRQA SGLQYHTTED STACIRAWQG
     VVKPAGELLR SEPAIIAALA KATLPDNPLM NWDAWVADYG LIREAIAGSY PEIFHDFNTR
     MLEPGGFHRP LGASQRQWAT DSGRANFMVP STLAVNDDVE PDPERRDVLN LMTVRSNDQF
     NTTVYGYNDR FRGIHGTRSV ILMHRNDMTR LALNEGDQVQ VSTAVDDGVQ RSVGPLRVTP
     HDIPEGCCAA YYPECNPLLP LWHHEEKAKV PAAKSIPVTL RRLIAMAQAR
//
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