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Database: UniProt
Entry: A0A2V4B2X9_9PSEU
LinkDB: A0A2V4B2X9_9PSEU
Original site: A0A2V4B2X9_9PSEU 
ID   A0A2V4B2X9_9PSEU        Unreviewed;       768 AA.
AC   A0A2V4B2X9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Molybdopterin-dependent oxidoreductase alpha subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BAY60_13870 {ECO:0000313|EMBL:PXY28387.1};
OS   Prauserella muralis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=588067 {ECO:0000313|EMBL:PXY28387.1, ECO:0000313|Proteomes:UP000249915};
RN   [1] {ECO:0000313|EMBL:PXY28387.1, ECO:0000313|Proteomes:UP000249915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45305 {ECO:0000313|EMBL:PXY28387.1,
RC   ECO:0000313|Proteomes:UP000249915};
RA   Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA   Schneider O., Winkler A., Zotchev S.B.;
RT   "Draft genome sequence of Prauserella muralis DSM 45305, isolated from a
RT   mould-covered wall in an indoor environment.";
RL   Submitted (JUL-2016) 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:PXY28387.1}.
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DR   EMBL; MASW01000002; PXY28387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4B2X9; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000249915; 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   GO; GO:0043546; F:molybdopterin cofactor 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; 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:UP000249915}.
FT   DOMAIN          125..510
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          654..759
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   768 AA;  83739 MW;  477AA4E0CE02B679 CRC64;
     MARNAPHDDI DEGRLEVGKP KEWAAGLPGV AVSLRRSWEQ MGAGRTVRTL RLLNQRDGYD
     CPGCAWPEPR EADGEHRKLA EFCENGAKAV AEEATTRRVG PEFFARHSVA ELAERSDYWL
     GQQGRLTHPM VLREGATHYE PVSWDEALRL TADALRGLSD PNQAIFYTSG RTSNEAAFAY
     QLLVRSFGTN NLPDCSNMCH ESSGAALTES TGIGKGTVSL ADVHHADLIV VIGQNPGTNH
     PRMLSALERA KAGGARVVAV NPLPEAGLMR FKNPQNVRGV LGKGSPLADE FCQIRLGGDL
     ALFQAIGHLL LTWDDAAPGT VLDHDFIGSS THDFADYAKQ LRELDWAEVE QATGVSREQI
     ARIASMIASS ERTVYCWAMG LTQHRHAVPT IREVANVALL RGMIGKPGAG LCPVRGHSNV
     QGDRTMGIWE KMPEEFLAAL EAEFGIDVPR EHGWDVVDSI RAMREGRGRV FFALGGNFAS
     ATPDTAATER ALRSCELTVH VSTKLNRSHA VTGRTALILP TLGRTERDVQ ASGEQFVTVE
     DSMSAVHASR GRIAPASEHL LSEVAILCRL ARELFGEAHP VPWREFEAGY DAIRDRIARV
     VPGCEDYNAR VREPDGFVLP NPPRDAREFT GTLTGKAMFS VNDLEYPRVP EGRLLLQTLR
     SHDQYNTTIY GLSDRYRGVE DGRRVVFVNP ADLAALGVAD GTLVDLVSEA DDGDRRAERF
     RVVSYPTAPG CAAAYFPEAN ALVPLDAVAR TSNTPASKAI VVRLEPTA
//
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