ID A0A267MGQ8_9CLOT Unreviewed; 1165 AA.
AC A0A267MGQ8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:PAB58736.1};
GN ORFNames=CCE28_13785 {ECO:0000313|EMBL:PAB58736.1};
OS Anaeromicrobium sediminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Anaeromicrobium.
OX NCBI_TaxID=1478221 {ECO:0000313|EMBL:PAB58736.1, ECO:0000313|Proteomes:UP000216024};
RN [1] {ECO:0000313|EMBL:PAB58736.1, ECO:0000313|Proteomes:UP000216024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY2726D {ECO:0000313|EMBL:PAB58736.1,
RC ECO:0000313|Proteomes:UP000216024};
RA Zeng X.;
RT "Draft genome sequence of anaerobic fermentative bacterium Anaeromicrobium
RT sediminis DY2726D isolated from West Pacific Ocean sediments.";
RL Submitted (JUN-2017) 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:PAB58736.1}.
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DR EMBL; NIBG01000012; PAB58736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267MGQ8; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000216024; 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; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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; SSF51905; FAD/NAD(P)-binding domain; 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:UP000216024}.
FT DOMAIN 2..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 606..639
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 645..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 1165 AA; 127825 MW; CCB707486311994F CRC64;
MAQIRLNIDG KEVIGHEGQT ILDIAKENDV YIPTLCYDSR VEIYGSCGLC VVEVEGIPKL
LRSCATKASD NMVVNTKSTR IKESRKTALE LLLSDHTGDC RPPCVLACPT NTDCQGYVGL
IANKQYDEAL KLIKEELPLP ASIGRVCPHP CEDACRRKLT DESISIAWLK SFVADIDLNG
VEKYMPEIKV STGKKVSIVG GGPGGLTAAY YLTKEGHDVT IYEAMPKLGG MLRYGIPEYR
LPKAVLDKEI QIIESMGAKL VPNTRLGKDL SFESLQESSD AVVLAIGAWN SSSMRCKGDD
LDGVMGGIDF LRKVVTNEHM KVGEKVAVVG GGNTAMDACR TAIRLGAKEV YNIYRRTEAE
MPAEEIEIVE GKEEGVIFKT LVNPIEVIGE DGKVSKIRLQ KMKQGEPDAS GRRRPIPIEG
EEETLDVDTV IVAIGQGVTP EGLDNVELTK WNTIIADENT FRTNLEGVFA IGDATNKGAS
IAIEAIGEGK KASHIINSYL HGKEVAYEKP YYVERNDLTE EDFADREKKH RPHMRHLLPE
ERNTNFNEIV EGYTEEQAIE EASRCLECGC HDYFECKLID YANDYNVAPD RLAGEVHNRK
VDNSHPFIDR NPDKCILCGL CVRVCDEVMG VGALGLVDRG FDTIVKPALD KPLKETNCIS
CGQCVSVCPT GALGEKSPIA KNVPLDTDES NHVCSHCSVG CNMTLHAKGD LVVRSVPNKD
SKVDNGLLCV KGRFGFDLHK HGEKIDSALV RKNGSLEKVD MNEGLLTAAK KIQSLKFLYG
SDSIGVSISD KYSNEEIHMI SRFAKEVIGT NNIFSFNKLS EGIKDVIGYD SSTSKYDELL
STDTILLVGA DMMKEFPVVG TKIKKAVKNN TKLLVINSES TTADEWAHNS FYPENNTLFL
NEVLKALVDL GAVPKNADNF NELKESLEGI TPSDEAKEIA NIYFNSKKAM IVFGQNNIST
SAAKLLANMA VVTNHIGCAR SGLIQLKPNC NSQGLSNLNI NGFESVVESI QDGNIKCLLT
FGENIPTCVD TSKLEFLVAL DQYTNDTTDS AHVVLPSAGL LESRGTYTNS EGTTQKINDH
KSLGKNIETV INLCNLLEYK INYINIDQIT EEVLSKYKSF SSGFNFEGGK AKLQVLSSDM
LFAKLDNTNN TTELFSKYLE SENLI
//
