GABAT_KLULA
ID GABAT_KLULA Reviewed; 472 AA.
AC Q6CJ86;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=4-aminobutyrate aminotransferase {ECO:0000250|UniProtKB:P17649};
DE EC=2.6.1.19 {ECO:0000250|UniProtKB:P17649};
DE AltName: Full=GABA aminotransferase {ECO:0000250|UniProtKB:P17649};
DE Short=GABA-AT {ECO:0000250|UniProtKB:P17649};
DE AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000250|UniProtKB:P17649};
DE Short=GABA transaminase {ECO:0000303|PubMed:24912400};
GN OrderedLocusNames=KLLA0F20548g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000312|Proteomes:UP000000598};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP PROBABLE FUNCTION, AND PATHWAY.
RX PubMed=24912400; DOI=10.1111/mmi.12666;
RA Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R.,
RA van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V.,
RA Wahl S.A., Pronk J.T., Daran J.M.;
RT "An alternative, arginase-independent pathway for arginine metabolism in
RT Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.";
RL Mol. Microbiol. 93:369-389(2014).
CC -!- FUNCTION: Required for the degradation of gamma-aminobutyric acid
CC (GABA), which is important for utilization of GABA as nitrogen source
CC and for oxidative stress tolerance. Deaminates GABA to succinate
CC semialdehyde, which in turn is converted to succinate by the succinate-
CC semialdehyde dehydrogenase UGA2 (By similarity). May be involved in an
CC alternative, arginase-independent arginine degradation pathway via GABA
CC (Probable). {ECO:0000250|UniProtKB:P17649,
CC ECO:0000305|PubMed:24912400}.
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:0000250|UniProtKB:P17649};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P17649};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation.
CC {ECO:0000305|PubMed:24912400}.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250|UniProtKB:P17649}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17649}.
CC -!- MISCELLANEOUS: Induced 4.7-fold in an arginase-negative strain during
CC exponential growth. {ECO:0000269|PubMed:24912400}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CR382126; CAG98711.1; -; Genomic_DNA.
DR RefSeq; XP_456003.1; XM_456003.1.
DR AlphaFoldDB; Q6CJ86; -.
DR SMR; Q6CJ86; -.
DR STRING; 28985.XP_456003.1; -.
DR PRIDE; Q6CJ86; -.
DR EnsemblFungi; CAG98711; CAG98711; KLLA0_F20548g.
DR GeneID; 2895485; -.
DR KEGG; kla:KLLA0_F20548g; -.
DR eggNOG; KOG1405; Eukaryota.
DR HOGENOM; CLU_016922_12_0_1; -.
DR InParanoid; Q6CJ86; -.
DR OMA; ATGKFWG; -.
DR UniPathway; UPA00073; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:0006527; P:arginine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:EnsemblFungi.
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; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..472
FT /note="4-aminobutyrate aminotransferase"
FT /id="PRO_0000432234"
FT BINDING 135..136
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 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 352
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 327
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
SQ SEQUENCE 472 AA; 52575 MW; FB2A97AAFE334999 CRC64;
MSVAAKYYPN EPTEPKVVTS EIPGPESKAK VASLGEVFDS RPAYFVADYA KSSGNYIVDV
DGNKFLDVYA QISSIALGYN NPALIEAAKS DKMIRALVDR PALGNFPGAD LEDILKQLLK
FAPKGQNKIW SGLSGADANE LAFKAAFMYY RQLQRGGHGI DFSEEENSSV MENTSPGSPQ
LAVLSFKKAF HGRLFASGSS TCSKPIHKLD FPAFNWPHGE YPVYKYPLSE NEEENKKEDD
RCLAIVEDLI KSWPTPVAAL IIEPIQSEGG DNHASKYFLQ SLRDLTSKYN VVYIIDEVQT
GVGATGKFWC HEWADIQPPV DLVTFSKKFQ SAGYWFHDDR FIPNKAYRQF NTWCGDPARM
IIAGAIGQEI VDNNLVDQCA RVGDYLFEKL EKLQAKYPTR LINLRGKNRG TFIAFDLETS
AERDQLLKLL KSNGCNVGGC AEKSVRLRPS LTFEEKHADI FVDALEKSIG QL
