ID G5DX79_SILLA Unreviewed; 646 AA.
AC G5DX79;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Molybdopterin biosynthesis protein CNX1 {ECO:0000256|RuleBase:RU365090};
DE AltName: Full=Molybdenum cofactor biosynthesis enzyme CNX1 {ECO:0000256|RuleBase:RU365090};
DE Includes:
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE Short=MPT Mo-transferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE AltName: Full=Domain E {ECO:0000256|RuleBase:RU365090};
DE Includes:
DE RecName: Full=Molybdopterin adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE Short=MPT adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.7.7.75 {ECO:0000256|RuleBase:RU365090};
DE AltName: Full=Domain G {ECO:0000256|RuleBase:RU365090};
DE Flags: Fragment;
OS Silene latifolia (White campion) (Bladder campion).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Sileneae; Silene;
OC Silene subgen. Behenantha; Silene sect. Melandrium.
OX NCBI_TaxID=37657 {ECO:0000313|EMBL:AEL99126.1};
RN [1] {ECO:0000313|EMBL:AEL99126.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Male and female bud flowers {ECO:0000313|EMBL:AEL99126.1};
RX PubMed=21889891; DOI=10.1016/j.cub.2011.07.032;
RA Bergero R., Charlesworth D.;
RT "Preservation of the y transcriptome in a 10-million-year-old plant sex
RT chromosome system.";
RL Curr. Biol. 21:1470-1474(2011).
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; JO495665; AEL99126.1; -; mRNA.
DR AlphaFoldDB; G5DX79; -.
DR UniPathway; UPA00344; -.
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 2: Evidence at transcript level;
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 Nucleotidyltransferase {ECO:0000313|EMBL:AEL99126.1};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AEL99126.1}.
FT DOMAIN 178..327
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 451..600
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEL99126.1"
FT NON_TER 646
FT /evidence="ECO:0000313|EMBL:AEL99126.1"
SQ SEQUENCE 646 AA; 68642 MW; 45E6D587DF522481 CRC64;
IAFEQALKYV LAVSERLEPE TLSLDQCLGK VLAQDILAPD PLPPHAASIK DGYAVVAADG
PGEYTVITES RAGNDALGVT VTSGTVAYVT TGGPIPDGAD AVVQVEDTEL IKSDSSESKR
VRILVQTRPG ADIRPVGCDI EKDDVVLNAG DLIGTSEIGL LATVGVTMVK VYRTPTVGIL
STGDELVEPT TINLQRGQIR DSNRAMLLAA AVEQRCKVVD LGIARDDEAE LEKIIDKAFA
AGVEIILSSG GVSMGDRDYV KPLLERRGKM HFTKVLMKPG KPLTFAEMNS KPSQNMKASK
VLAFGLPGNP VSCLVAFHLF VVPVIRCLSG WTNPDLLRVH ARLEQSIKAD PIRPEFHRAT
IKWKDNDGSG RPGFVAESTG QQMSSRLLSM KFANALLELP AGGRLLPPGT SVSAIVISDL
LSSVTKKEIA SQETPKGPAV TEFGDCAVQV AILTVSDTVA AGAGPDRSGP RAIAVINSAS
EKLGGAKVVA TAVVPDDIPK IKEILQRWSD VDKIDLILTL GGTGCTPRDV TPEATKEVIE
KETPGLLYVM MQESLKVTPF AMLSRSAAGI RGSTLIINMP GNPNAVAECM EALLPALKHG
LKQVKGDKRE KHPRHLPHAL AAPVDTWEKS YNKATGAEEH GCSCSH
//
