ID A0A2S0WPL4_9ACTN Unreviewed; 787 AA.
AC A0A2S0WPL4; A0A5F2EX23;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=FdhF/YdeP family oxidoreductase {ECO:0000313|EMBL:TGN34174.1};
GN ORFNames=C3E78_13770 {ECO:0000313|EMBL:AWB93184.1}, E4L97_03805
GN {ECO:0000313|EMBL:TGN34174.1};
OS Aeromicrobium chenweiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2079793 {ECO:0000313|EMBL:AWB93184.1, ECO:0000313|Proteomes:UP000244384};
RN [1] {ECO:0000313|EMBL:AWB93184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|EMBL:AWB93184.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000244384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=592 {ECO:0000313|Proteomes:UP000244384};
RA Li J.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TGN34174.1, ECO:0000313|Proteomes:UP000297606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S592 {ECO:0000313|EMBL:TGN34174.1,
RC ECO:0000313|Proteomes:UP000297606};
RA Li J., Ha Z., Lu H., Jin N.;
RL Submitted (MAR-2019) 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; CP026952; AWB93184.1; -; Genomic_DNA.
DR EMBL; SRPI01000001; TGN34174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WPL4; -.
DR KEGG; aez:C3E78_13770; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000244384; Chromosome.
DR Proteomes; UP000297606; 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; 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 119..519
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 641..749
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 735..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 86342 MW; 2FA338B022B042E9 CRC64;
MSKAKDIDED QLEVHAPKRA AAGVTGVRVA MQRSLSLMGP TRTARTLLKL NQTDGFDCVS
CAWPDPDPEN RHAAEFCENG AKAVADEATT DRVTPAFFAR HSIEEMAAHD DYWLNMQGRI
THPMVKRPGG THYEPIDWDD AYALIGEHLR TRESPDQATF YTSGRASNEA AFMYQLFTRA
YGTNNLPDCS NMCHESSGTA LTEAIGIGKG SVSLRDIYDA KCIVIAGQNP GTNHPRMLSA
LEIAKRRGAK IISVNPLREA GLVNFRNPQV PRGVVGKGTE IADLHLPIRL NGDLALFQGI
GRLLVEWDAL DHEFIDKHVD GFDSWREHVL AADWDEIEGA SGLTRDQIAE AAEIIRESDA
TIYCWAMGLT QHRNAVASIR EICNVALVRG DIGKRGAGLC PVRGHSNVQG DRTMGIWERV
PEHFLDSLQA EFGFDPPREH GLDTVDSIRG MRDGKITFFM GLGGNFVKAA PDTEVTADAL
ATTEMTVQVS TKLNRSHLEC GDTALILPTM GRTEHNATSA GEQFITVEDS MSAVHASRGV
IPPVSEHVRS EIAIIAGIAE ATIGDRHGIR WADMAEDYNI IRHHISRVVP GCEEYTHNVD
RPGGFVLPHA PRDTRTFETS SGKAELIASP LEVLQVPEGH LVLQTLRSHD QFNTTIYGLS
DRYRGIEDGR RVVFMHPDDI AAQGFKDRDM VDLVTRWDDD DVDRVAEKFR IVSYETPRGS
AAAYYPETNS LVPLDSTATG SNQPTSKSVI VRAVPAGQGR SDDTGGSQEG VGSDDSHKTD
RQPHHLS
//
