ID A0A238L283_9RHOB Unreviewed; 588 AA.
AC A0A238L283;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN Name=moeA_2 {ECO:0000313|EMBL:SMX48931.1};
GN ORFNames=PEV8663_04021 {ECO:0000313|EMBL:SMX48931.1};
OS Pelagimonas varians.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=696760 {ECO:0000313|EMBL:SMX48931.1, ECO:0000313|Proteomes:UP000220836};
RN [1] {ECO:0000313|EMBL:SMX48931.1, ECO:0000313|Proteomes:UP000220836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8663 {ECO:0000313|EMBL:SMX48931.1,
RC ECO:0000313|Proteomes:UP000220836};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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|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; FXYH01000019; SMX48931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238L283; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000220836; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; cd03116; MobB; 1.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR004435; MobB_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; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00176; mobB; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF03205; MobB; 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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|RuleBase:RU365090};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|RuleBase:RU365090};
KW Reference proteome {ECO:0000313|Proteomes:UP000220836};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SMX48931.1}.
FT DOMAIN 366..503
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 588 AA; 62496 MW; DB833CF1E93725A3 CRC64;
MKVFGVTGWK NAGKTGLMER LVAEITKRGF SVSTVKHAHH AFDVDHEGRD SYRHRVAGAH
EVMLASGVRI AQMSELRGSA EPPLSDLLAR LKPVDLVLIE GYKREPHPKI EAFREVAGHD
LMAPQDGTIA AVAADIALEV DLPVFDLDDT ARITEFVLRQ VGLIAEAQPT SNLKPPPLKN
DCFALPPGVN WTPVDEALEA LRTRLTTVVG RETVPLELAC GRVLAADLVA KRSNPPLPNT
AVDGYGFAGA VPEGEAVFPL IAGRSAAGVP YQGRVPDGHA IRVLTGAALP DGVDTVVLEE
DCAISETQIA FNGPVKHKSN TRKAGEDVAE GDIALSKGRV LTPADLALAA AVGFGELPVF
LPLRVGVLST GDELVEPGQE AGVGQIFDAN RPMLLSAIAR FGYKAVDLGR VADSRVALTD
QLKNAAAKVD VILTSGGASA GDEDHVSALL RESGALAEWR IALKPGRPLA LGIWDGVPVF
GLPGNPVAAF VCTLIFARPA LSVLAGSDWR VPDYFDVPAA FSKRKKPGRR EYLRARMRGG
RVEVFKSEGS GRVSGLSWAE GLVELGDEGR EISEGDLVRF YPYGSFGL
//
