ID D0WI60_SLAES Unreviewed; 467 AA.
AC D0WI60;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=HMPREF0762_01532 {ECO:0000313|EMBL:EEZ60727.1};
OS Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 /
OS KCTC 5966 / S-7).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=649764 {ECO:0000313|EMBL:EEZ60727.1, ECO:0000313|Proteomes:UP000006001};
RN [1] {ECO:0000313|EMBL:EEZ60727.1, ECO:0000313|Proteomes:UP000006001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 /
RC S-7 {ECO:0000313|Proteomes:UP000006001};
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., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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|ARBA:ARBA00002901, 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; EC=2.10.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001529};
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. {ECO:0000256|ARBA:ARBA00010763,
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:EEZ60727.1}.
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DR EMBL; ACUX02000016; EEZ60727.1; -; Genomic_DNA.
DR RefSeq; WP_006362794.1; NZ_GG700631.1.
DR AlphaFoldDB; D0WI60; -.
DR STRING; 649764.HMPREF0762_01532; -.
DR GeneID; 85008344; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_010186_7_1_11; -.
DR OrthoDB; 3196725at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000006001; 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 Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 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:UP000006001};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 209..355
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 372..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 49957 MW; C63629D6BEF2CA9E CRC64;
MRDHSKHIQL SREEAVARTL AMLDELPEGF GWRGALLQAA GASDDAATAH ARNVRRKLVE
RVSLAESIGR VLAYDVVAQN DMPSALTCAM DSIALHWSDF ADLPEGQLPD TGAWVRGVDW
QFANTGVAMP EGFDTAIVIE HAQVSADEQH IVIDAAPSKQ GAGTRPVGSS MRRGDVLAQA
GSIVTPDLAV RIGAGNNASV AVVRRPRVAF IPTGNELMTP GVPFDPAHTD SFAARGRTFE
TNSVLVRAKC EKWGGRFVPF DIVLDRRDTI EAALERAVEV ADIVVLNAGS SKGSDDWSCE
VMEEMGRMVC HQTNHGPGHH SSAAVIDGTP IVGISGPSGG ASFTLDFYLR PLMRAFMGLE
PEIGRTPAVL AEEFPPGGPG SAKKHGGPVR GEERPAEHPE HEPGTPEFYG VRMLRVEHAE
DGTLRAWPIA GFPGSAETLA ANAYCMLPMG PGIEAPRPGD VIRVEWR
//