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Database: UniProt
Entry: E8LDD1_9FIRM
LinkDB: E8LDD1_9FIRM
Original site: E8LDD1_9FIRM 
ID   E8LDD1_9FIRM            Unreviewed;       343 AA.
AC   E8LDD1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=HMPREF9443_00858 {ECO:0000313|EMBL:EFY05146.1};
OS   Phascolarctobacterium succinatutens YIT 12067.
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Phascolarctobacterium.
OX   NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY05146.1, ECO:0000313|Proteomes:UP000004923};
RN   [1] {ECO:0000313|EMBL:EFY05146.1, ECO:0000313|Proteomes:UP000004923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY05146.1,
RC   ECO:0000313|Proteomes:UP000004923};
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 (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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:EFY05146.1}.
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DR   EMBL; AEVN01000033; EFY05146.1; -; Genomic_DNA.
DR   RefSeq; WP_009145238.1; NZ_GL830875.1.
DR   AlphaFoldDB; E8LDD1; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_068847_1_0_9; -.
DR   OrthoDB; 9767940at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000004923; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03522; MoeA_like; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004923};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          173..308
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   343 AA;  37446 MW;  E07D3EDC9210B95B CRC64;
     MKLIRTEDAV GSVLCHDLTQ IIKGVTKDAV FRKGHVVQPE DIPVLLSIGK EHLYVWEADE
     NMLHENDAAR ILCDICKNTM MDESPVKEGK IELAAAADGL FKVDGARLRL VNSFGQMMIA
     TRHGNTPVKK GDKLCGTRII PLVIEKEKMQ RVRELCGDEP LLQLLPYKIK KAAVLATGSE
     VFHGRIKDTF TPVLEEKLAE FNVELVYKQV LDDKPEQIAA AIKTAIEEKG AEMVLCTGGM
     SVDPDDRTPL AIKNTGARIV SYGAPVLPGA MFLLSYYGEK QVPVMGLPGC VMYAKRTIFD
     LVLPRVLACD LVTADELAAL GEGGLCLNCA VCTYPACGFG KGW
//
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