ID   A9UZ37_MONBE            Unreviewed;       409 AA.
AC   A9UZ37;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=MONBRDRAFT_32367 {ECO:0000313|EMBL:EDQ89565.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ89565.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ89565.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000984};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CH991550; EDQ89565.1; -; Genomic_DNA.
DR   RefSeq; XP_001745594.1; XM_001745542.1.
DR   AlphaFoldDB; A9UZ37; -.
DR   STRING; 81824.A9UZ37; -.
DR   EnsemblProtists; EDQ89565; EDQ89565; MONBRDRAFT_32367.
DR   GeneID; 5890789; -.
DR   KEGG; mbr:MONBRDRAFT_32367; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   InParanoid; A9UZ37; -.
DR   OMA; PTWPIHE; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006533; P:aspartate catabolic process; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357}.
FT   DOMAIN          9..379
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   409 AA;  44906 MW;  87466FE3EACE3665 CRC64;
     MCKQDPDTSK LNLGVGAFRD DAGKPHVMTI VKEVEEEMAR EVAADTLNHE YPPMGGSQDL
     VMAAARLALG NDSSRIAHEH VTGVQALSGT GALRLNGEFL NLFHANKTIY IPDPTWGNHK
     PIFAESGLNV KTYRYFDEGT LGLDITGLLE DLAAAPKESI ILLHAVAHNP TGVDPTEEQW
     GMIADAIVAN DHLAVFDCAY LGFVSGDIDT DAMAMRLFAN RGLSFFICMS FSKNFGIYSE
     RCGVTLYVGA NPDEADAVVS QLKVIGRPMW SVPPMHGAHI VQRILLDEGR TAKWRYELKE
     QARRILRMRR ELYEGLKARD PAHNWDHIIN QSGMFTFTGL SKEQCDELIQ VHHVYLLDNG
     RINVSGIPAD RVDDLVDAIC AVVQPAPDAV SVCSLDMDSE ESPSASVSD
//