ID   B8HDP5_PSECP            Unreviewed;       456 AA.
AC   B8HDP5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 96.
DE   RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE            EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
DE   AltName: Full=Glutamate:succinic semialdehyde transaminase {ECO:0000256|ARBA:ARBA00050054};
DE   AltName: Full=L-AIBAT {ECO:0000256|ARBA:ARBA00029760};
GN   OrderedLocusNames=Achl_2798 {ECO:0000313|EMBL:ACL40763.1};
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL40763.1, ECO:0000313|Proteomes:UP000002505};
RN   [1] {ECO:0000313|EMBL:ACL40763.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A6 {ECO:0000313|EMBL:ACL40763.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001750};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde +
CC         L-glutamate; 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:0000256|ARBA:ARBA00048021};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005176}.
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; CP001341; ACL40763.1; -; Genomic_DNA.
DR   RefSeq; WP_015937959.1; NC_011886.1.
DR   AlphaFoldDB; B8HDP5; -.
DR   STRING; 452863.Achl_2798; -.
DR   KEGG; ach:Achl_2798; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000002505; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047589; F:5-aminovalerate:2-oxoglutarate transaminase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000013; 4-aminobutyrate aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000022; 4-aminobutyrate aminotransferase; 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; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   NCBIfam; NF004714; PRK06058.1; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ACL40763.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002505};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   456 AA;  47462 MW;  FE136C175CE4B821 CRC64;
     MTTTASDLTF RLEQKRNVQA DFPGPKSVAL TERRKSVVAA GVASSVPVYV ADADGGIIHD
     VDGNSFIDLG SGIAVTSVGA SDPAVVGAVK EAVEHFTHTC FMVTPYEGYV AVAEQLNRLT
     PGDHEKRTVL FNSGAEAVEN AVKVARLATG RDAVVAFDHA YHGRTNLTMA LTAKAMPYKT
     NFGPFAPEVY RMPMSYPFRE ENPSITGAEA AKRAITAIEK QIGGDQVAAI IIEPIQGEGG
     FIVPAEGFLP ALAAWAKDKG IVFIADEVQS GFCRTGEWFA VNHEGVVPDI ITMAKGIAGG
     MPLSAITGRA DLLDAVHPGG LGGTYGGNPV ACAAALASIG SMEEYDLNAR ARHIEELAVS
     RLSALQAELA GAGSAVIGDI RGRGAMLAIE LVQAGSKEPN PDLTKAVAAA CLKEGVIILT
     CGTYGNVIRL LPPLVITDDL LTDGLEVLAA AIKANA
//