ID A0A2U2MZ96_9GAMM Unreviewed; 646 AA.
AC A0A2U2MZ96;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=DEM34_13460 {ECO:0000313|EMBL:PWG62138.1};
OS Spiribacter halobius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG62138.1, ECO:0000313|Proteomes:UP000245474};
RN [1] {ECO:0000313|EMBL:PWG62138.1, ECO:0000313|Proteomes:UP000245474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E85 {ECO:0000313|EMBL:PWG62138.1,
RC ECO:0000313|Proteomes:UP000245474};
RA Zheng W.-S., Lu D.-C., Du Z.-J.;
RT "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT from marine solar saltern.";
RL Submitted (MAY-2018) 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:PWG62138.1}.
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DR EMBL; QFFI01000022; PWG62138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2MZ96; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000245474; 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: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 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:UP000245474};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 195..333
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 646 AA; 67714 MW; 48FD002B69B85187 CRC64;
MSDGAPEQRQ FLRAVSREEA LARLRAAFVP APLGVETVAL ETALGRVLAD DVAAAVDVPG
FDRANVDGFA VRAADTEDAA EDAPVQLALN AELLTPGIVP GVEVAPGTAT PIATGGMLPR
GADAVVMLEH SDRAGAGVAV TRPAAPGAFV THAGADIARG ESVLFAGQPL GSREIGLLAA
TGTGEVPVWR RPRVAILSTG DELLAPGEPP RDGGVYDSNG HILAAAVREH GGEPWALGIV
RDDEAALQAA IEQALAADMV LLSGGTSKGE GDIAHRVAGH WDDPGIVVHG VAVKPGKPLC
LAVTRGRPVV LLPGFPTSAI FTFQEFVAPV LRAMAGRREA MRSRRRATLP LALPSELGRA
EYHMVGLLPD ASGGLAAYPI PKGSGAVSTF SRADGFIVAG ERSRGLAAGS EVTVYCLDEA
QELPDVVAVG SHCVGLDRML ARLRREGYAV RSLHVGSLGG VEAARRGDCD VAGVHLLDPE
TDTYNRPWLP DGVRLLPGYR RRQGICYRAD DERLAGLAGT ALQTRLRADE ALVMVNRNAG
SGTRVLVDRL LGDWQPPGWG VQPASHNAVA AAVAQGRADW GVTIAPVAAA YGLAFDPLRD
EHYDFLVPES RWDRPAVARF RALLEDEAMR EELANVGMRV DGESGE
//
