ID A0A026WA63_OOCBI Unreviewed; 498 AA.
AC A0A026WA63;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
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};
GN ORFNames=X777_07159 {ECO:0000313|EMBL:EZA52982.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA52982.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA52982.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107295; EZA52982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WA63; -.
DR STRING; 2015173.A0A026WA63; -.
DR OMA; KTQVCGI; -.
DR Proteomes; UP000053097; 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EZA52982.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transferase {ECO:0000313|EMBL:EZA52982.1}.
SQ SEQUENCE 498 AA; 56135 MW; 5DF71DBC43321302 CRC64;
MFVNKCHRAL SARVLPRQLL NGATMWKRCL TGSVPREPDG PVVVTEIPGP RSRSLLQELN
AIQQASSVQF FADYEKSSGN YIIDVDGNAL LDVYMQISSM PLGYNHPAML ETLADPVNQK
IIANRPALGV FPGKDWPNKL RNVLLKKQVA PPGLSHITTM MCGSCSNENA FKNIFIWYAE
KQRQGTPFTK EEMVTCMMNQ SPGSPRYSIM SFKGAFHGRT LGCLSTTHSK YIHKMDIPAF
DWPIASFPEY KYPLAENVQE NQREDERCLA EVEELFEKYK NEKKVLVAGV IIEPIQAEGG
DNHASPEFFR GLQRVTRKHG AALLIDEVQT GGGPTGKMWC HEHFNLESPP DVMTFSKKMQ
LGGYYHTEDF KPKQSYRVFN TWMGDPSKVL LLESIMEIIR KENLLDRVTR VGDYMLKHLM
EIEREHSGIV NSVRGRGTFI AFNCTSPEMR DTVIKKLLAK GIQAGGCGSR AIRLRPALTF
TERHADIFLD ALRSTLKG
//
