ID A0A0D6ZAF3_9BACI Unreviewed; 639 AA.
AC A0A0D6ZAF3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN ORFNames=UB32_10765 {ECO:0000313|EMBL:KIY22031.1};
OS Mesobacillus subterraneus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY22031.1, ECO:0000313|Proteomes:UP000032512};
RN [1] {ECO:0000313|EMBL:KIY22031.1, ECO:0000313|Proteomes:UP000032512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY22031.1,
RC ECO:0000313|Proteomes:UP000032512};
RA Peet K.C., Thompson J.R.;
RT "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL Submitted (JAN-2015) 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 -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC {ECO:0000256|ARBA:ARBA00003487}.
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|ARBA:ARBA00005046, 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:KIY22031.1}.
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DR EMBL; JXIQ01000085; KIY22031.1; -; Genomic_DNA.
DR RefSeq; WP_044393678.1; NZ_JXIQ01000085.1.
DR AlphaFoldDB; A0A0D6ZAF3; -.
DR PATRIC; fig|285983.3.peg.717; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000032512; 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; cd00887; MoeA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 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; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR InterPro; IPR024370; PBP_domain.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF12727; PBP_like; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU365090};
KW Metal-binding {ECO:0000256|RuleBase:RU365090};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|RuleBase:RU365090};
KW Reference proteome {ECO:0000313|Proteomes:UP000032512};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 179..316
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 639 AA; 70436 MW; FDB8675F28EC1192 CRC64;
MDKIRYNRKI YLEDKPRAQA REEVLSAFDL PQKKEWIPAA AALGRITAEP VFAKVSMPFY
HASAMDGVAV NAEDTYEAHE QRPLQLKKDE QFTYVDTGNA IPQEFNAVIM VENIHVIDDE
TIEIIEPATP WQHIRPIGED IVQEEMLFTQ GHQLRPADLG ALLAAQATEV CVVKKPLVTI
IPTGNELVSA DASLSSGRII EFNGTVFSAY VEDWGGQPLL HPIVKDEPEK IREALLNAAD
TSEIVVINAG SSAGSKDYTV HILEELGTVF THGVATRPGK PVILGKIKEK VVVGVPGYPV
SAYMALEWFV RPLICKYLGV QEPERAKLKV KLGRRIVSTM GAEDFVRMNI GYVNGQFVAN
PLTRAAGVTM SLVRADGLLV VPPEELGYEQ GDTVEVELYR PVEEIKNAIV FSGSHDMTID
LLSSQLKNQR TDMKIVSSHV GSMAGLMAIR KGEAHVAGIH LLDPETKEYN ITYVRKLLAG
QDAVLYPFLK RTQGWMLPKG NPLGIEHVSD IAAKNADYAN RQKGAGTRIL FDLLLREAGL
DADQINGYDR EMFSHLSVAA EVKGNDNAAG LGIYPAARAM GLDFIPVADE SYDLLMTKAF
FESEKGRWLT SVIQSHAFQL EVDKIGGYAV VENPQPIYF
//
