ID A0A0L1JQV2_9RHOB Unreviewed; 693 AA.
AC A0A0L1JQV2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=ATO11_07560 {ECO:0000313|EMBL:KNG94092.1};
OS Pseudaestuariivita atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudaestuariivita.
OX NCBI_TaxID=1317121 {ECO:0000313|EMBL:KNG94092.1, ECO:0000313|Proteomes:UP000036938};
RN [1] {ECO:0000313|EMBL:KNG94092.1, ECO:0000313|Proteomes:UP000036938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z3 {ECO:0000313|EMBL:KNG94092.1,
RC ECO:0000313|Proteomes:UP000036938};
RA Li G., Lai Q., Du Y., Liu X., Sun F., Shao Z.;
RT "Aestuariivita atlantica sp. nov., isolated from deep sea sediment of the
RT Atlantic Ocean.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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}.
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:KNG94092.1}.
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DR EMBL; AQQZ01000003; KNG94092.1; -; Genomic_DNA.
DR RefSeq; WP_050530238.1; NZ_AQQZ01000003.1.
DR AlphaFoldDB; A0A0L1JQV2; -.
DR STRING; 1317121.ATO11_07560; -.
DR PATRIC; fig|1317121.7.peg.2119; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000036938; 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 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.
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:UP000036938};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 471..608
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 693 AA; 72797 MW; 2C680ED42266EF90 CRC64;
MTFDRIAMVD WSGGNDTGPT PRPDAIWIGT PEGPPDYLRN RQLAEDRLAG LIDDALTAGD
TLCLGFDFPF GYPAGFAAAL TGTADPFAVW HWLADRIEDA PKANNRFDVA ASINASMPGQ
GPFWANALKR DIPHLPRLKP ASIAFPERRV AEAQTSGAFT LWQLAGAGAV GSQALMGLPV
LARLRARFPD RIAVWPFDPL DRPVTFLEIW PSLLNDAVRR AMRVEGGVKD AVQVTTVARA
LAGLSAPDLS RLLDVTAPEE GWIFGLGHED VLADAARPRA PRLTNDCFAL PRGVDWLPVA
DALAHLRNAM RPVTAVTDEP LATAGGRRLA TDITALRANP PAANSAVDGY GFAGPAADGP
HRLPLLPGRA AAGAPFGGTV PPGHALRILT GALVPDGVDT VILDEDSSVS GGEIAFRGPL
KRGANVRKAG EDVTSGAPIL AQGLRLRPPD LALAAATGHA RLPVHAPLRV AVLSTGDEVT
DPAPDAPPSR TFDANRPMLL DLIARWGMTP VDLGRVPDDP AALTRALDRA TTEADAILTS
GGASAGDEDH VSALLGAQGT RHHWRIALKP GRPLALGQWG HLPVFGLPGN PVAALVCTLV
FARPALSVMA GGPWLDPTRL TLPASFTKSK KPGRTEYLRA RLTDAGVETF PSEGSGRISG
LSWATGLVEL GPDAATITPG TPVTYLPFAD LMS
//