ID   Q6N7D5_RHOPA            Unreviewed;       424 AA.
AC   Q6N7D5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CAE27764.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CAE27764.1};
GN   Name=goaT {ECO:0000313|EMBL:CAE27764.1};
GN   OrderedLocusNames=RPA2323 {ECO:0000313|EMBL:CAE27764.1};
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE27764.1, ECO:0000313|Proteomes:UP000001426};
RN   [1] {ECO:0000313|EMBL:CAE27764.1, ECO:0000313|Proteomes:UP000001426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA   Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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; BX572600; CAE27764.1; -; Genomic_DNA.
DR   RefSeq; WP_011157876.1; NZ_CP116810.1.
DR   AlphaFoldDB; Q6N7D5; -.
DR   STRING; 258594.RPA2323; -.
DR   GeneID; 66893382; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_5; -.
DR   PhylomeDB; Q6N7D5; -.
DR   Proteomes; UP000001426; Chromosome.
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:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00700; GABAtrnsam; 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; 2.
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:CAE27764.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001426};
KW   Transferase {ECO:0000313|EMBL:CAE27764.1}.
SQ   SEQUENCE   424 AA;  44855 MW;  AD2DF6B215D077E5 CRC64;
     MTNSELLTRR QTAVVRGVSQ ATPVFAERAL NSEIWDVEGK RYVDFAGGIA VLNTGHCHPR
     IVAAIREQLD RFTHTCFQVA PYEGYIRLAE RLNQLAPING PLKSILLSTG AEATENAVKI
     ARAATGRSGV IAFTGGFHGR TAFASAMTGK VIPYKKALGP PLPGVWHVPF PVAGSDVSVE
     DALRCVQFVF KADIDASQVA AIIIEPVQGE GGFHQAPPEL MRGLRRLCDE NGIVLIADEV
     QTGFGRTGKM FAMEHYDVQA DIVCVAKSLA GGLPLSGVIG RAAIMDAAEP GGLGGTYAGN
     PLACAAALAV LDVFEEENLI ARANQIGERL RSAIDRFALS NTLVPTSVAR GPGAMVAFDI
     LKQRGSNEPD AEATKRVTRL AHENGLILLS CGTAANTIRI LVPLTASDAI VDEGLAILER
     CLAA
//