ID A0A0B8NRR7_9NOCA Unreviewed; 419 AA.
AC A0A0B8NRR7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN Name=moeA {ECO:0000313|EMBL:APA95610.1};
GN ORFNames=NS07_v2contig00189-0002 {ECO:0000313|EMBL:GAM50953.1},
GN NS506_01539 {ECO:0000313|EMBL:APA95610.1};
OS Nocardia seriolae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM50953.1, ECO:0000313|Proteomes:UP000019401};
RN [1] {ECO:0000313|EMBL:GAM50953.1, ECO:0000313|Proteomes:UP000019401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N-2927 {ECO:0000313|EMBL:GAM50953.1,
RC ECO:0000313|Proteomes:UP000019401};
RA Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA Oshima S.;
RT "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT quinqueradiata) in Kochi Prefecture, Japan.";
RL Genome Announc. 3:e00082-15(2015).
RN [2] {ECO:0000313|EMBL:APA95610.1, ECO:0000313|Proteomes:UP000180166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM150506 {ECO:0000313|EMBL:APA95610.1,
RC ECO:0000313|Proteomes:UP000180166};
RA Han H.-J.;
RT "Genome sequence of Nocardia seriolae strain EM150506, isolated from
RT Anguila japonica.";
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017839; APA95610.1; -; Genomic_DNA.
DR EMBL; BAWD02000189; GAM50953.1; -; Genomic_DNA.
DR RefSeq; WP_033091306.1; NZ_RCNK01000180.1.
DR STRING; 37332.NS506_01539; -.
DR KEGG; nsr:NS506_01539; -.
DR PATRIC; fig|37332.12.peg.1570; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000019401; Unassembled WGS sequence.
DR Proteomes; UP000180166; 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:UP000019401};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:GAM50953.1}.
FT DOMAIN 187..326
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 419 AA; 44359 MW; 50DD3557540CA5A6 CRC64;
MRSVEDQQIK VTAAAVAPRP VRVAISEAQG LLCAEDVVTE RPLPGFDQAA IDGYAVRSVD
VAGAGANIRD EDGNSVDLSL PVVGEVAAGS RQPIRLQPRQ TVRVDTGAPL PTLADAVLPL
ENTDGGRARV KVYEPVRSGD YVRRIGDDVQ PGDLAVRAGT IIGPAQVGLL AAVGKDKVLV
HPRPRLSVLS VGGELVDIDR TPGPGQVYDV NSYSLAAAAR DAGADVNRVG IVSTDPKRLR
DVVEGQLVRS EVVVIAGAVG GWASEQVREA LEGLGELEIT RVAMHPGSVQ GFGLLGRDEV
PTFLLPSNPV GALVVFEVMV RPLIRIALGR RHPMRRVVRA RTILPIASIP GRRGYLRAQL
MRDEQTGDYL VQPLGGPNGA SSHLLATMAE ANSLIVIDPD VTEVRTGDEV RVAFLAQRG
//
