ID Q211A2_RHOPB Unreviewed; 424 AA.
AC Q211A2;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABD89034.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:ABD89034.1};
GN OrderedLocusNames=RPC_3494 {ECO:0000313|EMBL:ABD89034.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD89034.1};
RN [1] {ECO:0000313|EMBL:ABD89034.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD89034.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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; CP000301; ABD89034.1; -; Genomic_DNA.
DR AlphaFoldDB; Q211A2; -.
DR STRING; 316056.RPC_3494; -.
DR KEGG; rpc:RPC_3494; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_5; -.
DR OrthoDB; 9801834at2; -.
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:ABD89034.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABD89034.1}.
SQ SEQUENCE 424 AA; 44806 MW; 9990B0B2FB9DB590 CRC64;
MTNADLLTRR QAAVVRGVSH ATPIFAERAL NSEVWDVEGK RYVDFAGGIA VLNTGHCHPH
IVQAIRDQLD RFTHTCFQVL PYESYVELAE RLNALAPING PLKSILLSTG AEATENAVKI
ARAATGRSGV IAFTGSFHGR TAFASAMTGK VIPYKKLLGP PLPGVWHVPF PAAGGDVSVD
DALRAIAFIF KADIDASQVA AIIIEPVQGE GGFHQAPDEL MRGLRRICDE NGIVLIADEV
QTGYGRTGKM FAMEHFDVQA DIVCVAKSLA GGMPLSAVIG RAAIMDAAEP GGLGGTYAGH
PLACAAALAV LDVFEKENLV ARANQIGERL RAGIDRFALS NTLLPTSAAR GPGAMVAFDI
LKHRDSNEPD AAATKRVTKL AYENGLILLS CGTTANTIRI LVPLTASDAI IDEGLAILER
CLAA
//
