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Database: UniProt
Entry: G9YG56_9FIRM
LinkDB: G9YG56_9FIRM
Original site: G9YG56_9FIRM 
ID   G9YG56_9FIRM            Unreviewed;       216 AA.
AC   G9YG56;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Molybdenum cofactor synthesis domain protein {ECO:0000313|EMBL:EHM42486.1};
GN   ORFNames=HMPREF0080_00620 {ECO:0000313|EMBL:EHM42486.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM42486.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM42486.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM42486.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC       {ECO:0000256|ARBA:ARBA00003487}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046}.
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:EHM42486.1}.
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DR   EMBL; AGCJ01000018; EHM42486.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9YG56; -.
DR   STRING; 861450.HMPREF0080_00620; -.
DR   PATRIC; fig|861450.3.peg.595; -.
DR   eggNOG; COG0521; Bacteria.
DR   eggNOG; COG2258; Bacteria.
DR   HOGENOM; CLU_077358_1_1_9; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000005481; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR   PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   4: Predicted;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005481}.
FT   DOMAIN          1..47
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
SQ   SEQUENCE   216 AA;  23731 MW;  D50F775613BDA5D2 CRC64;
     MTQIGKECHA HCAVYHQVGD CIMPREGVFA KVLTGGVLHP GDELVIEERK ENRPYRAAVI
     TLSDKGSRGE RIDESGPVIV GELEKRGFEI TETLLLPDDE EQLKKQLVRL SDQRRLDIII
     TTGGTGFAPT DITPEATLAV ADRLVPGIAE AIRAESMRQT KRAIYSRAVS VLRKKTLIVN
     LPGSPKACRE CLAVFMDTVA HPLDLLRYGA SDCAEK
//
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