ID K0JQP8_SACES Unreviewed; 407 AA.
AC K0JQP8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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 Name=moeA1 {ECO:0000313|EMBL:CCH28006.1};
GN OrderedLocusNames=BN6_06780 {ECO:0000313|EMBL:CCH28006.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH28006.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH28006.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC ECO:0000256|RuleBase:RU365090}.
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DR EMBL; HE804045; CCH28006.1; -; Genomic_DNA.
DR RefSeq; WP_015098120.1; NC_019673.1.
DR AlphaFoldDB; K0JQP8; -.
DR STRING; 1179773.BN6_06780; -.
DR KEGG; sesp:BN6_06780; -.
DR PATRIC; fig|1179773.3.peg.682; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_010186_7_0_11; -.
DR OrthoDB; 9804758at2; -.
DR BioCyc; SESP1179773:BN6_RS03340-MONOMER; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000006281; Chromosome.
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; 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 PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 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.
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:UP000006281};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:CCH28006.1}.
FT DOMAIN 178..317
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 407 AA; 42642 MW; 8C550D55408910C4 CRC64;
MRSVDEQLAR VIAAAVRPAP VRVAISESQG LLCAEEVVAE RALPGFDQAA VDGYAVRSVD
VQAANDEPVQ LPVVGEITAG SRQPRRLQPG QAVRVATGAP LPTLADAVVP LGYTDGHPAK
VTVRRPVPSA GFVRRTGEDV QTGDVAVRRG ATIGAAQVGL LAAVGRNKVL VHPRPRVSVI
SIGEELVDVD RTPGQGQVYD VNSYALAAAA RDAGAEVSRV GIQSADPRRL REVVEGRLLL
SEIVVVAGGV GGVIGDEVRA ALADLGDVDS TRVAMHPGSV QGFGRLGPDA VPTFLLPANP
MSALVVFEVL VRPLIRAALG KRNPYRRAVS ARLLSPLTST KGRRGYLRGQ LLRDADNGEY
LVQPLGISGS HLLASLAEAN CLIMVDEDVT DVVVGEEVLV SFLAQKS
//
