ID A0A160P280_STRLU Unreviewed; 459 AA.
AC A0A160P280;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=SLA_3625 {ECO:0000313|EMBL:BAU84533.1};
OS Streptomyces laurentii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU84533.1, ECO:0000313|Proteomes:UP000217676};
RN [1] {ECO:0000313|EMBL:BAU84533.1, ECO:0000313|Proteomes:UP000217676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU84533.1,
RC ECO:0000313|Proteomes:UP000217676};
RA Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT ATCC 31255.";
RL Genome Announc. 4:e00360-16(2016).
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; AP017424; BAU84533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160P280; -.
DR KEGG; slau:SLA_3625; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000217676; 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; 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:UP000217676};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 229..367
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 46686 MW; A46BE2458EB0B6DD CRC64;
MTSDERGSDD GMDEALALVG RRPRPAGPAG QDPASGPAVP PPQTSPGHRH GTAWPEARAA
AARAGTTAAA TRRPVPVPLG QALGRVLAEP LRALTDLPSF DTSAMDGWAV AGPGPWRTAP
EGPEGSVLAG HATTAELADG HAVRIATGAR VPAGATAVVR AEHSRTDAAG QLHARREVVQ
GQDIRPRGQE CRSGDRLMPA GSLVTPAVLG LAAAAGYDEL TTYPRPRVEV LVLGDELLTS
GLPHEGLIRD ALGPLLDPWL CALGADVLGV RRIGDDAEEL YRAVTGSAAD VVVTTGGTAS
GPVDHVHPVL AKAGATLLVD GVRVRPGHPM LLAALGDPAD RYLVGLPGNP LAAVSGLLTL
AEPLLRALAG HPAAGSVPFS VPVRDGIQGH PQDTRLVPVL DRDGAAVPLR YSGPAMLRGI
ATADGMAVVP PGGARPGQAL DVLDLPWTAP ATGQGVCFT
//
