ID A0A0S8ECY1_9CHLR Unreviewed; 383 AA.
AC A0A0S8ECY1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE Flags: Fragment;
GN ORFNames=AMJ77_06645 {ECO:0000313|EMBL:KPK45938.1};
OS Dehalococcoidia bacterium SM23_28_2.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703396 {ECO:0000313|EMBL:KPK45938.1, ECO:0000313|Proteomes:UP000054036};
RN [1] {ECO:0000313|EMBL:KPK45938.1, ECO:0000313|Proteomes:UP000054036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_2 {ECO:0000313|EMBL:KPK45938.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK45938.1}.
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DR EMBL; LJUA01000089; KPK45938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8ECY1; -.
DR STRING; 1703396.AMJ77_06645; -.
DR PATRIC; fig|1703396.3.peg.1033; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000054036; 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 Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 147..287
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPK45938.1"
SQ SEQUENCE 383 AA; 41208 MW; 4B9AA00F6AD91A15 CRC64;
PPLDNSAMDG YALQAASTVG ASPSAPVELG VIGELAAGYV FEGEVTPDTA VRIMTGAPVP
KAADAVVPFE DTEEAVHRAP RTARRLDEAV RILREARPGD NIRRAGEDIH EGQRVLAKGV
ILRPAEIGML ASVGRTTVKV IRRPVVAVLS TGDELVEVGQ TLPPGRIYDS NSYSVAALIQ
RYGGIPRVLG IAPDTVEALV AKIRQGLDAD MLLTSAGVSR GDYDMVKDVL VREGEIDFWT
VAMKPGKPLA FGLFRSGQRR IPHIGLPGNP VSSMVSFELF ARPAILKMMG KTNWQKPLIR
AVAKERIVNR NDPRRYFARC IVTEEDGRYY ASLTGPQGSG ILSSMAAANA LTVIPEDVDV
VEPGDEITVM MLDWSQGSEW STA
//
