ID   Q2IVC7_RHOP2            Unreviewed;       424 AA.
AC   Q2IVC7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABD07833.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABD07833.1};
GN   OrderedLocusNames=RPB_3137 {ECO:0000313|EMBL:ABD07833.1};
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD07833.1, ECO:0000313|Proteomes:UP000008809};
RN   [1] {ECO:0000313|EMBL:ABD07833.1, ECO:0000313|Proteomes:UP000008809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2 {ECO:0000313|EMBL:ABD07833.1,
RC   ECO:0000313|Proteomes:UP000008809};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000250; ABD07833.1; -; Genomic_DNA.
DR   RefSeq; WP_011442017.1; NC_007778.1.
DR   AlphaFoldDB; Q2IVC7; -.
DR   STRING; 316058.RPB_3137; -.
DR   KEGG; rpb:RPB_3137; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_5; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000008809; 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:ABD07833.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABD07833.1}.
SQ   SEQUENCE   424 AA;  44768 MW;  09AA4F13DB1FC940 CRC64;
     MTNSELLARR HEAVVRGVSQ ATPIFAERAL NSEIWDVEGK RYIDFAGGIA VLNTGHCHPR
     VVEAVRGQLD RFTHTCFQVL PYESYIRLAE RLNALAPING PLKSILLSTG AEATENAVKI
     ARAATGRSGV IAFTGGFHGR TAFASAMTGK VIPYKKALGP PLPGVWHAPF PAAGGDVTVE
     DALRCVSFIF KADIDASQVA AIIIEPVQGE GGFHQAPPEL MRGLRRICDE SGIVLIADEV
     QTGFGRTGKM FAMEHYDVQA DIVCVAKSLA GGMPLSGVIG RAAIMDAAEP GGLGGTYAGN
     PLACAAALAV LDVFEDENLI ARANQIGERL RNAIDRFALS NTLVPTSAAR GPGAMVAFDI
     LKQRGSSEPD AETTKRVTRL AYENGLILLS CGTAANTIRI LVPLTASDAI VDEGLAILER
     CLAA
//