ID A0A238YP39_9PSEU Unreviewed; 649 AA.
AC A0A238YP39;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=SAMN06265360_11675 {ECO:0000313|EMBL:SNR73036.1};
OS Haloechinothrix alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Haloechinothrix.
OX NCBI_TaxID=664784 {ECO:0000313|EMBL:SNR73036.1, ECO:0000313|Proteomes:UP000198348};
RN [1] {ECO:0000313|EMBL:SNR73036.1, ECO:0000313|Proteomes:UP000198348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45207 {ECO:0000313|EMBL:SNR73036.1,
RC ECO:0000313|Proteomes:UP000198348};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZNW01000016; SNR73036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YP39; -.
DR OrthoDB; 3196725at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000198348; 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 InterPro; IPR024370; PBP_domain.
DR NCBIfam; TIGR00177; molyb_syn; 1.
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:UP000198348};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 181..318
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 649 AA; 68356 MW; 4CE0FE78FB64D94E CRC64;
MQDSPFISDV PAESAIQAWR RACLSHGCAE RTDTVTVALA DAVGRVTAEP VWANRSSPVG
DVAAMDGIAV RARDTHGASE TTPLWLAPGS YEVVDTGDPM PEQRDAVIMR EHVHYVASGS
GESAEILAAV PPYHNVRSIG EDVSAGELLL PEGHRLRPVD VAAAAAAGAT ELTVRRTPRV
AVIPTGDEIV PIGSPPRQDE IVDTNSLMLA AQAREAGCEA WTTAVQPDDT GRIGAAVRDA
SATADLVIVI AGSSAGRDDY TARVISEQGT LAVHGVAVRP GHPVVLGAVD AAPVIGVPGY
PVSAALTFDI FAAPMLAELE GAAPPHRPET RARLARKLPS VVGMDDWVRV RLGSVGGTVV
ATPLPRGAGV LTSLVRADGL LFVPAAVEGH HPGEEVSVQL LRRYPEIERT IVAIGSHDLV
LDLAANALRS SDPTLTLASS NVGSLGGLVA LRDGLCHIAG SHLLHPSTGE YTLPYLDEMM
PDRELAVVRL VHRDQGLLVP PGNPHGITGL HDLVERDLSY VNRQRGAGTR MLLDHELHCR
EIDPQRISGY AREEPTHLAV AAAVSAGRAD CGLGILAAAR AFGLDFVPVA QEPYDLVLDA
NTLDDPLLAP LWELLDSPAF QASIRELGGY DTEETGRVVH RSGRARPAT
//
