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Database: UniProt
Entry: F0KLQ8_ACICP
LinkDB: F0KLQ8_ACICP
Original site: F0KLQ8_ACICP 
ID   F0KLQ8_ACICP            Unreviewed;       802 AA.
AC   F0KLQ8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Oxidoreductase molybdopterin {ECO:0000313|EMBL:ADY82662.1};
GN   Name=ydeP {ECO:0000313|EMBL:ADY82662.1};
GN   OrderedLocusNames=BDGL_002076 {ECO:0000313|EMBL:ADY82662.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY82662.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY82662.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY82662.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(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; CP002177; ADY82662.1; -; Genomic_DNA.
DR   RefSeq; WP_014207424.1; NC_016603.1.
DR   RefSeq; YP_004996344.1; NC_016603.1.
DR   AlphaFoldDB; F0KLQ8; -.
DR   STRING; 871585.BDGL_002076; -.
DR   GeneID; 11636595; -.
DR   KEGG; acc:BDGL_002076; -.
DR   PATRIC; fig|871585.3.peg.2077; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_6; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000007477; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007477}.
FT   DOMAIN          122..502
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          665..772
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   802 AA;  89089 MW;  1C9C4CE5A15EFDF6 CRC64;
     MDNSEEQKHI QENNGFARIE PYTHPAGGWG ALLSVARNLK RQDILGKGSI TLLNINQPTG
     FDCPGCAWPE KKDAHAFNFC ENGAKAVAFE ATSKTVTPEY FAGHTVSWLS EQSDFFLEDL
     GRLTDPVRYD AATDKYVPIS WDDAFKLIAQ HLHALDNPDQ AAFYTSGRAS NEAAFLYQLF
     VRSFGTNNFP DCSNMCHETT SVGLLDSIGL GKGTVTLEDF DVADAIFSFG HNPGTNHPRM
     LGTLREVSKR GGNIIAINPI KERGLERFQD PQAPLEMMTN GSTPISRYYF QPKIGGDYAL
     MLGMLKHLNE WDKKALASGK PSVFDRNFIA VNTVGFDEMI AEIERTEWAD IYKHSGLSPE
     HLEKLAKLFL ESERSIFCWG MGITQHRHGT ANVHMLANLL LARGQIGRPG AGLCPVRGHS
     NVQGDRTMGI NELPSPKLLD NIDRVFGIKS PRKNGHGVVE TIKAMAEGEV KVFIGLGGNF
     AVATPDTPYT QEALRKCNLT VHVATKLNRS HLVCGKDALI LPCLGRTEID EQLHGPQAIS
     VEDSMSNIHL SAGRNAPISD NILSEPDIVA RMAEAVLPDS QIKWKWYIES YDRIRDSIAD
     VFDEFHDFNL RVYKPGGFHL EHPANQHIWN TKSGKAQFMI TPLSEVYADK ENQYAAAYTD
     SKVYTLMTTR SHDQYNTTLY GLDDRYRGVF GQRRVLFMNQ ADIDEAGFEA NQWVDIESVF
     SDGVKRIVHS FRIVPYNIPR GSLAAYYPET NPLVALSSHD KYAKIPASKS VPVILHPGNA
     PEHFNLATAV APEDADKKVS SL
//
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