ID A0A0N8GPG4_9CHLR Unreviewed; 656 AA.
AC A0A0N8GPG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=ADN00_01130 {ECO:0000313|EMBL:KPL80826.1};
OS Ornatilinea apprima.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Ornatilinea.
OX NCBI_TaxID=1134406 {ECO:0000313|EMBL:KPL80826.1, ECO:0000313|Proteomes:UP000050417};
RN [1] {ECO:0000313|EMBL:KPL80826.1, ECO:0000313|Proteomes:UP000050417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3M-1 {ECO:0000313|EMBL:KPL80826.1,
RC ECO:0000313|Proteomes:UP000050417};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Ornatilinea apprima DSM 23815.";
RL Submitted (JUL-2015) 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:KPL80826.1}.
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DR EMBL; LGCL01000003; KPL80826.1; -; Genomic_DNA.
DR RefSeq; WP_075061126.1; NZ_LGCL01000003.1.
DR AlphaFoldDB; A0A0N8GPG4; -.
DR STRING; 1134406.ADN00_01130; -.
DR PATRIC; fig|1134406.4.peg.1971; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000050417; 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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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 InterPro; IPR024370; PBP_domain.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF12727; PBP_like; 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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 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:UP000050417};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 189..332
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 656 AA; 70832 MW; D2541223FF7F1F68 CRC64;
MPVYLHDIPL ETAQAHFNKA LERAGLGGRL GEEEVLMDEK SIGRVLSQPV WAKICSPHYH
ASAMDGFAVR AEATAGASPA TPVMLETGSQ TAYVDTGDPL PEWANAVVPI EQVESLDAED
RAAENVRDPL FIRLRQAATP WAHVRLMGED IVATQLVLPE GHVLRPVDLG AIAGAGYSAV
MVSRKPRVAV LPTGTELVEI GEPIKRGDII EYNSVVIAAQ VTQWGGEATR YPITPDRFDL
LKQRVQEAAD QFDLVLVNAG SSAGSEDFTS RIVEGLGELL VHGVAVRPGH PVILGLIRRS
DDSRSVPVIG IPGFPVSAAL TGEIFVEPLL ARWLGRQPNQ PLEIDASLTR KITSPAGDDD
FMRVVVGKVG ERTLAAPLSR GAGVITSLVR ADGIALVPRG IQGLEAGSPV RVKLYRHPAE
VEKTIFAIGS HDLTLDLLAQ YLTRYGRRLV SANVGSLGGL VALRRQEAHL AGSHLLDPES
GEYNISYLRQ YLPDTPVRLM TWVEREQGLV VKRGNPKGIQ SLCDLSRDDV SFVNRQRGAG
TRVLLDYHLQ KLSIDPAVIK GYELEEFTHL AVAVAVASGR ADCGMAVAAA ADALELDFVP
LYPERYDLVI PCQYLENDLL SPIFDLAADA GFRTAVAGLR GYSVKKMGNL VLDCSK
//
