ID R6EPH6_9FIRM Unreviewed; 1153 AA.
AC R6EPH6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Molybdopterin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN497_01851 {ECO:0000313|EMBL:CDB02483.1};
OS Firmicutes bacterium CAG:145.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263005 {ECO:0000313|EMBL:CDB02483.1, ECO:0000313|Proteomes:UP000018044};
RN [1] {ECO:0000313|EMBL:CDB02483.1, ECO:0000313|Proteomes:UP000018044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:145 {ECO:0000313|Proteomes:UP000018044};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CDB02483.1}.
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DR EMBL; CBCX010000047; CDB02483.1; -; Genomic_DNA.
DR AlphaFoldDB; R6EPH6; -.
DR STRING; 1263005.BN497_01851; -.
DR Proteomes; UP000018044; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 4: Predicted;
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:UP000018044}.
FT DOMAIN 2..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 606..625
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 650..678
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 687..743
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1153 AA; 124949 MW; C317D5DB19A1F1C2 CRC64;
MNKFRLNING KEVTGVAGQT ILEVARENDI FIPTLCYDER TKIYGSCGLC MCEVEGNPKL
CKACATEIAP GMVIRTNTER VIESRKTNLE LLLSNHTGDC RPPCVLACPG QTDCQGYVGL
IANGEYEKAL ELIKDKIPLP AALGRVCPHP CEEACRRGLI DEPISIQQLK RFAADVDLEG
EVFVPECEED TGKSVAIIGG GPMGLSAAYF LRQMGHDVTI FESMPNAGGM LRYGIPEYRL
PKAVLDEEIA TIESMGVEII TNTKVGVDIP FETVRSDYDA VLLGIGAWVS TGVGCKGEDA
EGVIGGIDFL RRVVRNEEIG MGRKVAIVGG GNTAMDACRT AVRLGAEEVY NIYRRTKDEM
PADMVEIEEA EEEGVIFKNL TNPIEVVKDE NGHVKEVVLQ VMELGEPDAS GRRKPVPVEG
KTETLAIDTM ILAIGQAVDA TVFDCDKTRK NAIAYDPDTF MTSIPGVFAG GDCGNDKISI
AIEAIADARK AADSIDAYLY GEVLKYEKPY VVERDDITEK TFEDRERMCR PEIPQLSPEE
RKDNFSEVIP EGFTEEQAVA EASRCLECGC HDYFECKLID FANQYDVHPE RFAGEKSTIE
FEDDHPFIVR DPNKCILCGL CVRVCDEVMG VGALGLVHRG FDTVVKPNME KPLIESGCIS
CGQCVSVCPT GALQERTTMI KETPVETEVT DTTCSYCSVG CSLKLETCGD MLIKANPDKD
GTVNKGLACG KGKWGFDCSM LEDKLEDPLV KEDGTFRDAD YHEAFVLVAK KCQSVAAKYG
KDSIAVAISD RYTNEEAYAM KKMAEAMGAK VLCMNNRASG LKAVTGLDAS PNTIDELLST
NLILRIGFKD EDSRVITLKM KQAEEAGAKV INLCSGENSV GFLKEIAKAI IDSGKAKKVA
GYDEFAASVA SVKVSDEAKA IADQYLAAKK AMIVYQQNFL TVAGATLIAD IAMLSGHIGT
PRDGILQVKA KNNSQGLIDM GITAGKEALE GVKALVVFGE NADIDTEALE FLAVCDTHMT
ELGAKADVVI PGTGFASVDG TFTNTERRMQ LVEAAIDEDI LFSNWEVAAE IAHVFEVDFE
WEGTDDISDE MSDTVDAYKY AQLNEVLGGV LKPADGAALV AVADGPVVEE LPCTDSLMQI
IMQRLPKPAN PTA
//
