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Database: UniProt
Entry: A0A369S716_9METZ
LinkDB: A0A369S716_9METZ
Original site: A0A369S716_9METZ 
ID   A0A369S716_9METZ        Unreviewed;       327 AA.
AC   A0A369S716;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Biotin--protein ligase {ECO:0000313|EMBL:RDD42697.1};
GN   ORFNames=TrispH2_004865 {ECO:0000313|EMBL:RDD42697.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD42697.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD42697.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD42697.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD42697.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062};
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:RDD42697.1}.
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DR   EMBL; NOWV01000050; RDD42697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369S716; -.
DR   STRING; 287889.A0A369S716; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd03144; GATase1_ScBLP_like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR019197; Biotin-prot_ligase_N.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002161; PdxT/SNO.
DR   PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR   PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR   Pfam; PF09825; BPL_N; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 2.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:RDD42697.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843}.
FT   DOMAIN          66..325
FT                   /note="Biotin-protein ligase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09825"
SQ   SEQUENCE   327 AA;  36445 MW;  AE0E625135F576FB CRC64;
     MESGIHMLDY WCRERKADRL TPGLWTVAGD QCIRPLLGYN RRQHSKCNIT TERTNSGDCI
     MSQRKILIYC DDGSANVDVA EASIKQAINE LHLQNDFQIE NVTANDIIGN ENTLLSTKLF
     VMPGGRDLPY VEKLNGQGNR RIKHFVNQGG CYLGLCAGAY FASSIIEFEK DTALEVCGAR
     ELKFYHGLAK GCVYPGFSYK DNSGARVVPI ELHKEIADQV SFNQCSVYYN GGCEFLPLND
     DVGEVEILAS YSAHDNENSS VNRHAPPIAI IKCKVGSGIA ILSGVHPEYS ANLLSPDKYD
     DKILQHLHQC EHNRAVLFRK LLSMLLL
//
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