ID A4TDD7_MYCGI Unreviewed; 757 AA.
AC A4TDD7;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=Molybdopterin dinucleotide-binding region {ECO:0000313|EMBL:ABP46926.1};
GN OrderedLocusNames=Mflv_4457 {ECO:0000313|EMBL:ABP46926.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46926.1};
RN [1] {ECO:0000313|EMBL:ABP46926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46926.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP46926.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46926.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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 -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP000656; ABP46926.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TDD7; -.
DR STRING; 350054.Mflv_4457; -.
DR KEGG; mgi:Mflv_4457; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR OMA; CGLNIEV; -.
DR OrthoDB; 7376058at2; -.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 757 AA; 81911 MW; FEEBA69E79FEC4D8 CRC64;
MEHRVTCPLC EAMCGLKITV SDGVATSARG NADDVWSRGH LCPKGASLHQ IHHDPDRLRL
PLVRSRSGEH VQVSWDDAFT ETERVLRPVI DRYGARAVTV YLGNPVAHNL GLQTYIGALV
GMAGAVGMPA YYTPGTVDQW PLNVVSALLF GGMWNAPIPD LDRTDHLMML GANPSASQGS
MLSAPDIMGR LAAIRARGGT VVVVDPRRTP TARRASEWVP VHPGTDALLL FAILHTLAER
GWIRRPPHLQ DLVAGLDDVV GLAARFSPER VEVATGVPAG TVRRLAADLA AAERPVLYSR
IGACTQEFGT LATWLVFVLN VALGSVDAPG GALFPKAAVW SPMFMKPPDQ DGPGWRFGRF
HSRVRRVPEV LGQFPVSCLA EEIDTPGDGQ IRGLITVAGN PVISAPGSRR LDAALSGLDA
MISVDNWLNE TSRHAHVVLP GLSPLERAHC DDLYWMYSVA SCVKWTEPVF PTRPDRPQEW
EILLRLAGAV LGTAVPDVDV RAMDDLYSQG IIHTACQADD TPLSGRDPGE VFEALDGVGP
ERMTDLGIRV GPWGDDLGRR PGGLTLDEVR RHPDGLRLAE LEGGRLPDVL TTPSRRIELL
HPLLEADIPR LVSRIDRGRD DLVLTSRRHL RSNNSWMHNV AALMRGKDRC TLLIHPDDAL
RHDVADGGQV EVSTTEGSIV VVAEVSDEMM PGVVCLPHGW GHGIDGTRLA VANAHPGVNS
NLLSPPALVD VPSNTQVVNG VPCRLRSRRE PPHASAR
//