GABT_DICDI
ID GABT_DICDI Reviewed; 495 AA.
AC Q55FI1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=4-aminobutyrate aminotransferase;
DE EC=2.6.1.19;
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
GN Name=gabT; ORFNames=DDB_G0268104;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P80147};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P80147}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73505.1; -; Genomic_DNA.
DR RefSeq; XP_647552.1; XM_642460.1.
DR AlphaFoldDB; Q55FI1; -.
DR SMR; Q55FI1; -.
DR STRING; 44689.DDB0231448; -.
DR PaxDb; Q55FI1; -.
DR EnsemblProtists; EAL73505; EAL73505; DDB_G0268104.
DR GeneID; 8616360; -.
DR KEGG; ddi:DDB_G0268104; -.
DR dictyBase; DDB_G0268104; gabT.
DR eggNOG; KOG1405; Eukaryota.
DR HOGENOM; CLU_016922_12_0_1; -.
DR InParanoid; Q55FI1; -.
DR OMA; DPPDMVT; -.
DR PhylomeDB; Q55FI1; -.
DR Reactome; R-DDI-916853; Degradation of GABA.
DR PRO; PR:Q55FI1; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; ISS:dictyBase.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..495
FT /note="4-aminobutyrate aminotransferase"
FT /id="PRO_0000327473"
FT BINDING 160..161
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 374
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT MOD_RES 350
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
SQ SEQUENCE 495 AA; 55692 MW; D79738D198B10CE1 CRC64;
MSSSRLIKCL SSNNYIVRSF SKSSIPTTPT PDFPGEYKEP IVKTQIPGPQ SKALIERLNK
LQDPRAAHFF ADYANSRGNY ISDVDGNILL DLYCQIASIP IGYNNPELIK AAKSDRWVSA
IINRPSLGVL PPKDWPALIE NSFMQVSPKG LNQVFTAMCG SCANECAYKA VFMHYQHVKR
GGKPFTPEEL SSCMKNQEPG SPSLSILSFK KGFHGRTFGT LSTTRSKAIH KLDIPAFDWP
AATFPDLKYP LAEHAKENRE IEDRCLQEVE QLIKTWHIPV AGIIVEPIQA EGGDNYATPY
FFQGLRDITK KHGVSMIVDE VQTGMGATGK FWAHEHWNLT SPPDIVTFSK KMQAAGFYHN
LDYRPSESYR NFNTWMGDPV RALELEVVIG EIKKNHLLDN VVITGNYLKD GLFDIAARYP
GLIQNIRGEG TFLAIDFPTP AERDRVISHI RLLGVEMGGC GERSIRFRPM LVCQPSHINQ
FLNRFDQTMK ELYKN
