ID B3SED2_TRIAD Unreviewed; 341 AA.
AC B3SED2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV18915.1};
GN ORFNames=TRIADDRAFT_34461 {ECO:0000313|EMBL:EDV18915.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV18915.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV18915.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV18915.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; DS985432; EDV18915.1; -; Genomic_DNA.
DR RefSeq; XP_002118601.1; XM_002118565.1.
DR AlphaFoldDB; B3SED2; -.
DR STRING; 10228.B3SED2; -.
DR EnsemblMetazoa; TriadT34461; TriadP34461; TriadG34461.
DR GeneID; 6759814; -.
DR KEGG; tad:TRIADDRAFT_34461; -.
DR CTD; 6759814; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_016922_4_3_1; -.
DR InParanoid; B3SED2; -.
DR OMA; YTMPPYV; -.
DR OrthoDB; 3641488at2759; -.
DR PhylomeDB; B3SED2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00508; bioA; 1.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV18915.1"
SQ SEQUENCE 341 AA; 39029 MW; CC89A3AD8B20202B CRC64;
DLRHIWHPCS QMKDYEDMDA LLIKKANGSY IEMHSGKKII DAISSWWCKL LGHNHPYIKS
KVIEQINKFE HVIFAGTTNE KIVELSERLA ARSRNLQKVF YVGDGSCAVE VALKMSLHSR
KIKKQHKKNK FIALKNGYHG ETVGALSVSD LGIYKNPYDN LLFDVHLISD IPYINSKKDL
LWDDCSSYWY KIQEKLEKIK NEVTAIIFEP IVQGAEGMKI YSKDFLVKLR KWASENEIHL
IADEIMTGIC RTGKFFACEY ADIEPDFMCL SKGLTSGWIP FSAAMIKDEI YDIFYNDYSP
ENSFLHSHTY CGNPIAVSAA LATLDVIEND NILAKVDILR K
//
