ID   A0A163MRP2_ABSGL        Unreviewed;       437 AA.
AC   A0A163MRP2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=4-aminobutyrate transaminase {ECO:0008006|Google:ProtNLM};
GN   Name=ABSGL_13579.1 scaffold 14267 {ECO:0000313|EMBL:SAM07921.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM07921.1};
RN   [1] {ECO:0000313|EMBL:SAM07921.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM07921.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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; LT554871; SAM07921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163MRP2; -.
DR   STRING; 4829.A0A163MRP2; -.
DR   InParanoid; A0A163MRP2; -.
DR   OMA; GREWIDF; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:UP000078561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   437 AA;  47237 MW;  1B72F3DE2BC20218 CRC64;
     MLSSSSSSFN EKKQALGKGI TVSSDLVVDR AQECVITMTN GEDYLDMTSG IGVASTGHCH
     PTVVKAVQDQ VAKMSHAQIN MFYHTPLLTL MDRLRPYTAP LDTFCFNNSG SEAVESAVKL
     ARHATKKQNI IVFNGGHHGR TIGAMALTGS KTMFSAGFGP LMSGVYYVDY PYSFRCPSAG
     FEGHAPDHCG KEVMRQLETL LQQRCHPDDT AAVLIEPVLG EGGYVPAPKG FFQALRTFCD
     HHNILMIADE VQTGFGRTGK MFAINHWDTV PDILVMAKGI ASGYPLSGIV AKRALMDLQP
     PGSMGGTFVG NIVATAAAVA TLDVFEQENV LQNVQERSEQ VFKRLRCQAD RLPFGPVDIR
     GLGLMIGLEF AGAPKGFAAQ VVKHAREQEH LLLLTASIYE TIRMIPPLVV DGATLDDAVD
     RLVRSIVHVA GEMGAKI
//