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Database: UniProt
Entry: A0A0J6WWW3_9FIRM
LinkDB: A0A0J6WWW3_9FIRM
Original site: A0A0J6WWW3_9FIRM 
ID   A0A0J6WWW3_9FIRM        Unreviewed;       312 AA.
AC   A0A0J6WWW3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Molybdenum cofactor biosynthesis protein {ECO:0000313|EMBL:KMO86332.1};
GN   ORFNames=AB840_08555 {ECO:0000313|EMBL:KMO86332.1};
OS   Megasphaera cerevisiae DSM 20462.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO86332.1, ECO:0000313|Proteomes:UP000036503};
RN   [1] {ECO:0000313|EMBL:KMO86332.1, ECO:0000313|Proteomes:UP000036503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO86332.1,
RC   ECO:0000313|Proteomes:UP000036503};
RA   Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA   Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA   Samadpour M.;
RT   "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT   type strain 20462.";
RL   Submitted (JUN-2015) 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:KMO86332.1}.
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DR   EMBL; LEKT01000025; KMO86332.1; -; Genomic_DNA.
DR   RefSeq; WP_048514421.1; NZ_LEKT01000025.1.
DR   AlphaFoldDB; A0A0J6WWW3; -.
DR   STRING; 39029.BSR42_07610; -.
DR   PATRIC; fig|1122219.3.peg.1412; -.
DR   InParanoid; A0A0J6WWW3; -.
DR   OrthoDB; 9784492at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000036503; 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   Pfam; PF03473; MOSC; 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:UP000036503}.
FT   DOMAIN          18..142
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
SQ   SEQUENCE   312 AA;  33657 MW;  EEA5B11373E6D056 CRC64;
     MGTVKAICIS HVRGIQKTPV ATGRFVPDWG VDGDAHAGHW HRQVSLLALE RIEAFRQKGV
     DVPYGAFGEN LVVAGFDFAS LPVGTLLRCG DVLLEMTQIG KECHNHCAIY QAVGDCIMPR
     EGVFARVLAG GTIQAGDPME IEKRQGRRLY QAAVITLSDR GSRGEREDQS GPVIVRRLTA
     AGYEVVETLI LPDDKEKLTA QLCRLADQRQ IDLILTTGGT GFSPRDMTPE ATKAAADREV
     PGIAEAIRAA SLKITKRAML SRAVSVIRGH SLIINLPGSP QACQECMDVF LDTVPHGLDV
     LRGAVGDCAR AR
//
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