ID A0A1Q9JFN0_9FIRM Unreviewed; 1171 AA.
AC A0A1Q9JFN0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:OLR54999.1};
GN ORFNames=BHK98_02245 {ECO:0000313|EMBL:OLR54999.1};
OS Hornefia porci.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR54999.1, ECO:0000313|Proteomes:UP000187404};
RN [1] {ECO:0000313|EMBL:OLR54999.1, ECO:0000313|Proteomes:UP000187404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-3-10 {ECO:0000313|EMBL:OLR54999.1,
RC ECO:0000313|Proteomes:UP000187404};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR54999.1}.
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DR EMBL; MJIE01000001; OLR54999.1; -; Genomic_DNA.
DR RefSeq; WP_075712007.1; NZ_MJIE01000001.1.
DR AlphaFoldDB; A0A1Q9JFN0; -.
DR STRING; 1261640.BHK98_02245; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000187404; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster 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; 1.
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; 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; 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; 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:ARBA00023014};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000187404}.
FT DOMAIN 2..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 607..640
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 651..679
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 688..744
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1171 AA; 128026 MW; 9BF98B5BB1AF2432 CRC64;
MKKFRMNIDG KEVFGLPGQT ILEVARENDI FIPTLCYDER TKIYGACGIC VVEVEGNPKL
CKACATDIAD GMVVMTSTER VLESRKTNLE LLVSNHNGDC KGPCSLACPA GTDCQGYVGL
IANGEYEKAN ELIKDKIPLP ASIGRVCPHP CEDDCRRALV DEPISIMALK RFAADNDLMA
EEQYLPEIDE PTGKSVAIIG GGPMGLSAAY FLRQMGHEVT IFDAMPKLGG MLRYGIPEYR
LPKEVLDSEI ELIRAMGVEI VPDTKVGEDI PFETVRGDFD AVLLGIGAWV STGVGCPGED
AEGVIGGIDF LRKVVRNEPI DFGEKVAIVG GGNTAMDACR TAVRMGAKEV YNIYRRTKDE
MPADMLEIEE AEEEGVIFKN LTNPKEILKD ENGHVKQVVL QCMELGEPDE SGRRRPVPVE
GKTETIDIDT VILAIGQAVD ASIFDVDKTR KNAIAYDPDT YMTSMPGVFA GGDCGNDKIS
IAIEAIADAK KASEVIDSYL NGETIKYEKP FFVERDDITE KTFEDRERIC REKADQLSAA
ERKDNFSEVV FGGLTEEQAV KEANRCLECG CHDYYECKLI ELSNQYGVKS DRFCGEKNLT
EFEDDHPFIA RDTDKCILCG LCVRVCDEVM GVGALGLVNR GFDTVVMPNM MKPLAESGCE
SCGQCVACCP TGALQEKQTV QKEVPLDTEI TETTCSYCSV GCSLDLESYG DMLIKANPDE
EGYVNAGICC AKGKWGFDAS VLEGKIVDPR IKDGDGFRLT DYHEAFVMMA KKLEAVRVRH
GAESIGVAIS DRYTNEEAYA IKKFADVIGA RTFTFNRRAS GVSEVLGLDH EASPNTIDEL
LSTDVILVPG FIKNRNAVIW NKIKQAAERG ASVIVLNTEG AQDEWEFAAK VINVDNSTEF
LKRIAKYLVE NGKTSDAEGF DAFVKSLEGV ELCDECRSVA EMYAGAKKAM IVYQQNVLST
EAARLIGEIA MLSGHIGTPR DGILEVKPKN NSQGLVDLGI YAGAEAMDGL KGLLIFGEDP
TDADLSGLEF LGVSDVMMTE TAKKADVVLP GTGFASASGT YTNTERRLMP VEPAIDEDVD
FSNWEIAAEL AHVFEEEFSF EDEYDISEEM NDAVPMYKYA EEGEILGGAL KPCEPKFRAA
EDAKLIDELA CTDAMMRQTA ERIPTPVKAT I
//
