ID T1JB58_STRMM Unreviewed; 622 AA.
AC T1JB58;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=MoaB/Mog domain-containing protein {ECO:0000259|SMART:SM00852};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR010991-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR010991-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC molybdate is inserted into adenylated molybdopterin and AMP is
CC released. {ECO:0000256|RuleBase:RU365090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; Evidence={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;
CC Evidence={ECO:0000256|RuleBase:RU365090};
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.
CC {ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; JH432008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JB58; -.
DR STRING; 126957.T1JB58; -.
DR EnsemblMetazoa; SMAR010991-RA; SMAR010991-PA; SMAR010991.
DR eggNOG; KOG2371; Eukaryota.
DR HOGENOM; CLU_010186_2_2_1; -.
DR OMA; RHRESPY; -.
DR OrthoDB; 275356at2759; -.
DR PhylomeDB; T1JB58; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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 CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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 NCBIfam; TIGR00177; molyb_syn; 2.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
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; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 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:UP000014500};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 15..161
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 393..530
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 622 AA; 67426 MW; C8BC150BBBFEA25E CRC64;
MSNTSLDSTI PLEIGLLTIS DRCSRGESQD ISGLNIRNIL QSTEELANVI VIQSIVADDQ
VVIETTLKSW CDQLQLGLIL TIGGTGFAPR DVTPEATKNV IEKEAPGMAL AMLKGSLEVT
PMAMLSRSAC GIRGQTLIVN LPGSKKASDE CLQFVLPCLH HATSLLRNDN SEIESTHDRM
SCSHDFSFCT SKYSLEDSAD GQVAFRARKS PYPAIPVRTA VDNILRETKI LDFETLNYKD
AHGRVLAIDV RAKDPLPPFP ASVKDGYAVI AADGVGIRKV LGESSAGSSD CSEIKPGCCL
RINTGAPVPS GANAVVQVED TELVIASEDG VKEIEVNILK APNVGLDIRP IGCDIQVKEK
VLKAGTTVGS FELGILAAVG QTQVTVYKRP KIALMCPEDH ELLPGHIRDS NTLTLTSLLQ
EHGFSKVITD ILRDSPDEIE EKLKTIFQNV DVIITTGGVS MGDKDFLKQV LKNSFNADIH
FGRVFMKPGL PTTFATVTVS NKKKLIFCLP GNPVSATVTF HLFVLPALYH MTGHVKPPIP
KIKAKLGFEV PHLDPRPEYQ RVILHWPEDS ETPVAKSTGA QRSSRLVSMV RANAIVILPP
RTESQAKLEK GTVVNALLLR KL
//