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Database: UniProt
Entry: A0A091HPJ8_CALAN
LinkDB: A0A091HPJ8_CALAN
Original site: A0A091HPJ8_CALAN 
ID   A0A091HPJ8_CALAN        Unreviewed;       485 AA.
AC   A0A091HPJ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=4-aminobutyrate aminotransferase, mitochondrial {ECO:0000256|ARBA:ARBA00015937};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE            EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
DE   AltName: Full=L-AIBAT {ECO:0000256|ARBA:ARBA00029760};
DE   Flags: Fragment;
GN   ORFNames=N300_08895 {ECO:0000313|EMBL:KFO98198.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO98198.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO98198.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO98198.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-
CC         oxopropanoate + L-glutamate; Xref=Rhea:RHEA:13993, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57700, ChEBI:CHEBI:58655; EC=2.6.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00033650};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13994;
CC         Evidence={ECO:0000256|ARBA:ARBA00033650};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00033680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC         Evidence={ECO:0000256|ARBA:ARBA00033680};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
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; KL217734; KFO98198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091HPJ8; -.
DR   STRING; 9244.A0A091HPJ8; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; 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; IPR004631; 4NH2But_aminotransferase_euk.
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   NCBIfam; TIGR00699; GABAtrns_euk; 1.
DR   PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO98198.1"
FT   NON_TER         485
FT                   /evidence="ECO:0000313|EMBL:KFO98198.1"
SQ   SEQUENCE   485 AA;  54558 MW;  15F382747BBCB399 CRC64;
     LCFTGHRYIS QAAAKIDVDF DYDGPLMKTE VPGPRSRVSI MAWSLIVFSF KNAEGVHFFC
     NYEESRGNYL VDVDGNRMLD LYSQISSIPI GYSHPSLIKL LQQPQNLSTF INRPALGILP
     PENFADKLKE SLLSVAPKGL SQVVTMSCGS CSNENAFKAI FMWYRNKERG HNNVTKEELE
     SCMINQPPGC PDYAMLSFMG GFHGRTMGCL ATTHSKAIHK LDIPSLDWPI APFPRLKYPL
     EDFVKENQQE EARCLEEVED LIVKYRKKKK IVAGIIVEPI QSEGGDNHAS DDFFRKLRDI
     ARKHGCAFLV DEVQTGGGCT GKFWAHEHWG LDDPADVVTF SKKMMTGGFF SKEEFRPNAP
     FRIFNTWLGD PSKNLMLAEV IKVIKTEDLL NNATHAGKAL LTGLLDLQAR YPHLISRVRG
     RGTFCSFDTP NDATRNKLIT IARNKGVVLG GCGDRSIRFR PTLIFKDHHA HLFLNIFSDI
     LANFK
//
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