GABT_BACSU
ID GABT_BACSU Reviewed; 436 AA.
AC P94427;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable 4-aminobutyrate aminotransferase;
DE EC=2.6.1.19;
DE AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE EC=2.6.1.22;
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
DE AltName: Full=Glutamate:succinic semialdehyde transaminase;
DE AltName: Full=L-AIBAT;
GN Name=gabT; Synonyms=ycnG; OrderedLocusNames=BSU03900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; D50453; BAA09021.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12198.1; -; Genomic_DNA.
DR PIR; C69764; C69764.
DR RefSeq; NP_388272.1; NC_000964.3.
DR RefSeq; WP_003234459.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P94427; -.
DR SMR; P94427; -.
DR STRING; 224308.BSU03900; -.
DR PaxDb; P94427; -.
DR PRIDE; P94427; -.
DR EnsemblBacteria; CAB12198; CAB12198; BSU_03900.
DR GeneID; 938264; -.
DR KEGG; bsu:BSU03900; -.
DR PATRIC; fig|224308.179.peg.413; -.
DR eggNOG; COG0160; Bacteria.
DR InParanoid; P94427; -.
DR OMA; TSGQMSC; -.
DR PhylomeDB; P94427; -.
DR BioCyc; BSUB:BSU03900-MON; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IMP:CACAO.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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; IPR004632; 4NH2But_aminotransferase_bac.
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; TIGR00700; GABAtrnsam; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..436
FT /note="Probable 4-aminobutyrate aminotransferase"
FT /id="PRO_0000120383"
FT MOD_RES 281
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 47249 MW; D0961F6D4189A8F3 CRC64;
MSQTTASITT AQWQQKRDQF VSKGVSNGNR SLAVKGEGAE LYDLDGRRFI DFAGAIGTLN
VGHSHPKVVE AVKRQAEELI HPGFNVMMYP TYIELAEKLC GIAPGSHEKK AIFLNSGAEA
VENAVKIARK YTKRQGVVSF TRGFHGRTNM TMSMTSKVKP YKFGFGPFAP EVYQAPFPYY
YQKPAGMSDE SYDDMVIQAF NDFFIASVAP ETVACVVMEP VQGEGGFIIP SKRFVQHVAS
FCKEHGIVFV ADEIQTGFAR TGTYFAIEHF DVVPDLITVS KSLAAGLPLS GVIGRAEMLD
AAAPGELGGT YAGSPLGCAA ALAVLDIIEE EGLNERSEEI GKIIEDKAYE WKQEFPFIGD
IRRLGAMAAI EIVKDPDTRE PDKTKAAAIA AYANQNGLLL LTAGINGNII RFLTPLVISD
SLLNEGLSIL EAGLRA