ID A0A1S2HVP7_9MICO Unreviewed; 408 AA.
AC A0A1S2HVP7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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=BIU97_14895 {ECO:0000313|EMBL:OII15214.1};
OS Curtobacterium sp. MCBA15_009.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898737 {ECO:0000313|EMBL:OII15214.1, ECO:0000313|Proteomes:UP000180289};
RN [1] {ECO:0000313|EMBL:OII15214.1, ECO:0000313|Proteomes:UP000180289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_009 {ECO:0000313|EMBL:OII15214.1,
RC ECO:0000313|Proteomes:UP000180289};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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}.
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:OII15214.1}.
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DR EMBL; MJGO01000005; OII15214.1; -; Genomic_DNA.
DR RefSeq; WP_071253662.1; NZ_MJGO01000005.1.
DR AlphaFoldDB; A0A1S2HVP7; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000180289; 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; 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:UP000180289};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 190..328
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 408 AA; 40432 MW; D82A140FA7A50AE6 CRC64;
MRTIGQHRDD LAALLAPVLA GLGAEQCAVD ELAAGSSAGA GWRVLAAPVV SPVPLPPFDN
SQMDGFAVRA ADAGDTVRVV EPIPAGVVPE PLAPGTAAPI MTGARIPTGA DAVFPVEATG
PGAFPAALDL PQVTVPGDLT AGTFVRTTGS DLATGAELAP AGAVVTPALL GALASAGVST
VSVRRPLRVL VVSTGSELQG ADVDAATIGD ANGTALRAAL AEVGAGSRAV RVPDDVPSFV
GALDAAVGSW ADLVLTTGGI SAGAYEVVRQ ALEPRGLAVT PVAMQPGGPQ ASGTVVLAGR
PLPVVSFPGN PVSALVSFEV FLRPLLAPLV GLPAERPAQR LPAAAAAASP PGKHQVRRGR
VADGLVHLVG GPGSHLLAHH AAATHLVHVP VGVDAVEPGD ELTVWSLR
//
