GenomeNet

Database: UniProt
Entry: G3T201_LOXAF
LinkDB: G3T201_LOXAF
Original site: G3T201_LOXAF 
ID   G3T201_LOXAF            Unreviewed;       663 AA.
AC   G3T201;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Gephyrin {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};
GN   Name=GPHN {ECO:0000313|Ensembl:ENSLAFP00000007161.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007161.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000007161.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007161.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000007161.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007161.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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|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   AlphaFoldDB; G3T201; -.
DR   STRING; 9785.ENSLAFP00000007161; -.
DR   Ensembl; ENSLAFT00000008529.3; ENSLAFP00000007161.3; ENSLAFG00000008524.3.
DR   eggNOG; KOG2371; Eukaryota.
DR   GeneTree; ENSGT00390000016577; -.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; G3T201; -.
DR   OMA; RHRESPY; -.
DR   TreeFam; TF300902; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0043546; F:molybdopterin cofactor binding; IEA:Ensembl.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:Ensembl.
DR   GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IEA:Ensembl.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
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; 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; 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   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:UP000007646};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          1..99
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          472..615
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          115..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  71637 MW;  F6148A64EB3AEC8D CRC64;
     QETLIDWCDE KELNLILTTG GTGFAPRDVT PEATKEVIER EAPGMALAML MGSLNVTPLG
     MLSRPVCGIR GKTLIINLPG SKKGSQECFQ FILPALPHAI DLLRDAIVKV KEVHDELEDL
     PSPPPPLSPP PTTSPHKQTE DKGVQCEEEE EEKKDSGVAS TEDSSSSHIT AAAIAAKKHP
     FYTSPAVVMA HGEQPIPGLI NHSHHATHSA DERIPDSIIS RGVQVLPRDT ASLSTTPSES
     PRAQATSRLS TASCPTPKVQ SRCSSKENIL RASHSAVDIT KVARRHRMSP FPLTSMDKAF
     ITVLEMTPVL GTEIINYRDG MGRVLAQDVY AKDNLPPFPA SVKDGYAVRA ADGPGDRFII
     GESQAGEQPT QTVMPGQVMR VTTGAPIPCG ADAVVQVEDT ELIRESDDGT EELEVRILVQ
     ARPGQDIRPI GHDIKRGECV LAKGTHMGPS EIGLLATVGV TEVEVNKFPV VAVMSTGNEL
     LNPEDDLLPG KIRDSNRSTL LATIQEHGYP TINLGIVGDN PDDLLNALNE GISRADVIIT
     SGGVSMGEKD YLKQVLDIDL HAQIHFGRVF MKPGLPTTFA TLDIDGVRKI IFALPGNPVS
     AVVTCNLFVV PALRKMQGIL DPRPTIIKAR LSCDVKLDPR PEYHRCILTW HHQEPLPWAQ
     STG
//
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