ID A8ANL8_CITK8 Unreviewed; 427 AA.
AC A8ANL8;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CKO_04009 {ECO:0000313|EMBL:ABV15081.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV15081.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV15081.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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; CP000822; ABV15081.1; -; Genomic_DNA.
DR RefSeq; WP_012134773.1; NC_009792.1.
DR AlphaFoldDB; A8ANL8; -.
DR STRING; 290338.CKO_04009; -.
DR GeneID; 45137656; -.
DR KEGG; cko:CKO_04009; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000008148; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008148};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 427 AA; 45681 MW; 0FFBC780DBCA2BCA CRC64;
MSSNKELMHR RSNAVPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP
EIVSAVEAQL KKLSHTCFQV LAYEPYLELC ELMNQKVPGD FAKKTLLVTT GSEAVENAVK
IARAATKRSG AIAFSGAYHG RTHYTLSLTG KVNPYSAGMG LMPGHVYRAL YPCALHGISD
DDAIASIQRI FKNDAAPEDI AAIIIEPVQG EGGFYAASPA FMQRLRALCD EHGIMLIADE
VQSGAGRTGT LFAMEQTGVA PDLTTFAKSI AGGFPLAGVT GRADVMDAIP PGGLGGTYAG
NPLACAAALA VLNIFEQENL LQKAKDLGQT LRKGLLNIAE THREIGDVRG PGAMIAIELF
ENGDRSKPDA KLTADIVARA RDKGLILLSC GPYYNVLRIL VPLTIEEAQI QQGLDIIAQC
FDEAKQG
//
