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Database: UniProt
Entry: A0A0A1V8S3_9HYPO
LinkDB: A0A0A1V8S3_9HYPO
Original site: A0A0A1V8S3_9HYPO 
ID   A0A0A1V8S3_9HYPO        Unreviewed;       468 AA.
AC   A0A0A1V8S3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EXV05956.1};
GN   ORFNames=X797_000673 {ECO:0000313|EMBL:EXV05956.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV05956.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV05956.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV05956.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:EXV05956.1}.
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DR   EMBL; JELW01000001; EXV05956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1V8S3; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_10_0_1; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000030151; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
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   ECO:0000313|EMBL:EXV05956.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EXV05956.1}.
SQ   SEQUENCE   468 AA;  50890 MW;  ABD3E79C2FC14440 CRC64;
     MAPGIVTKDM ASTSMMVFPI EEDMPPTLYQ NIDEKALVAK SKKHLLDYGT KFEPDVITGC
     RGLYIYTASG HKLLDWTSGQ MSCLLGHGHP EIVKVITDHA MQLDHLFSGM VSPPVISLAD
     RLCNALPAGL DKAFFLSTGG ESNEAAIKMA KTYTGKFEIV GIGASWHGVT AQALGAQYHF
     GRRGHGPLMP GMHMLPAPNA YRSIFRKPNG SYDWEAELEY GWRMIDLQSC GSLAACIVEC
     IQSSGGMHVL PPGYLKALKK QCEMRGMLLI VDEAQTGVGR CGDFMAINHE NVVPDILTLS
     KTLGNGLPLS AVVTSDEVAS VAAEKGFFFY TTHVNDPLPA AVGDKVLEIL FRDNLIEHSR
     KCGEILHNGL QKLHSRYGCI GQVRGRGLMA GVEIVTDRES KRPALELAKR VGNRAYELGL
     WANLSSHPSF GGTFRIAPPI TVTESQVEDG LAILERAFAE TEGTLPLY
//
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