GABAT_SCHPO
ID GABAT_SCHPO Reviewed; 474 AA.
AC O13837;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=4-aminobutyrate aminotransferase;
DE EC=2.6.1.19 {ECO:0000269|PubMed:17355287};
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
GN Name=uga1; ORFNames=SPAC19D5.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=17355287; DOI=10.1111/j.1742-4658.2007.05729.x;
RA Andersen G., Andersen B., Dobritzsch D., Schnackerz K.D., Piskur J.;
RT "A gene duplication led to specialized gamma-aminobutyrate and beta-alanine
RT aminotransferase in yeast.";
RL FEBS J. 274:1804-1817(2007).
CC -!- FUNCTION: Required for the degradation of gamma-aminobutyric acid
CC (GABA), which is important for utilization of GABA as nitrogen source.
CC Deaminates GABA to succinate-semialdehyde, which in turn is converted
CC to succinate by the succinate semialdehyde dehydrogenase. Cannot
CC transaminate beta-alanine (BAL). {ECO:0000269|PubMed:17355287}.
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:0000269|PubMed:17355287};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P17649};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17355287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16717.1; -; Genomic_DNA.
DR PIR; T37967; T37967.
DR RefSeq; NP_594905.1; NM_001020336.2.
DR AlphaFoldDB; O13837; -.
DR SMR; O13837; -.
DR BioGRID; 278953; 3.
DR STRING; 4896.SPAC19D5.07.1; -.
DR MaxQB; O13837; -.
DR PaxDb; O13837; -.
DR PRIDE; O13837; -.
DR EnsemblFungi; SPAC19D5.07.1; SPAC19D5.07.1:pep; SPAC19D5.07.
DR GeneID; 2542494; -.
DR KEGG; spo:SPAC19D5.07; -.
DR PomBase; SPAC19D5.07; uga1.
DR VEuPathDB; FungiDB:SPAC19D5.07; -.
DR eggNOG; KOG1405; Eukaryota.
DR HOGENOM; CLU_016922_12_0_1; -.
DR InParanoid; O13837; -.
DR OMA; DPPDMVT; -.
DR PhylomeDB; O13837; -.
DR BRENDA; 2.6.1.19; 5613.
DR Reactome; R-SPO-916853; Degradation of GABA.
DR PRO; PR:O13837; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IDA:PomBase.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:PomBase.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IDA:PomBase.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:PomBase.
DR GO; GO:0019740; P:nitrogen utilization; ISO:PomBase.
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 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..474
FT /note="4-aminobutyrate aminotransferase"
FT /id="PRO_0000120380"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..143
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 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 357
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 333
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
SQ SEQUENCE 474 AA; 52945 MW; 2B92B232BADEF4E4 CRC64;
MSSTATVTES THFFPNEPQG PSIKTETIPG PKGKAAAEEM SKYHDISAVK FPVDYEKSIG
NYLVDLDGNV LLDVYSQIAT IPIGYNNPTL LKAAKSDEVA TILMNRPALG NYPPKEWARV
AYEGAIKYAP KGQKYVYFQM SGSDANEIAY KLAMLHHFNN KPRPTGDYTA EENESCLNNA
APGSPEVAVL SFRHSFHGRL FGSLSTTRSK PVHKLGMPAF PWPQADFPAL KYPLEEHVEE
NAKEEQRCID QVEQILTNHH CPVVACIIEP IQSEGGDNHA SPDFFHKLQA TLKKHDVKFI
VDEVQTGVGS TGTLWAHEQW NLPYPPDMVT FSKKFQAAGI FYHDLALRPH AYQHFNTWMG
DPFRAVQSRY ILQEIQDKDL LNNVKSVGDF LYAGLEELAR KHPGKINNLR GKGKGTFIAW
DCESPAARDK FCADMRINGV NIGGCGVAAI RLRPMLVFQK HHAQILLKKI DELI
