ID   A8GJW0_SERP5            Unreviewed;       421 AA.
AC   A8GJW0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABV43400.1};
GN   OrderedLocusNames=Spro_4306 {ECO:0000313|EMBL:ABV43400.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV43400.1};
RN   [1] {ECO:0000313|EMBL:ABV43400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV43400.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV43400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GJW0; -.
DR   STRING; 399741.Spro_4306; -.
DR   KEGG; spe:Spro_4306; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9801052at2; -.
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; 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   ECO:0000313|EMBL:ABV43400.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABV43400.1}.
SQ   SEQUENCE   421 AA;  45151 MW;  629BBFA9B5F4C21B CRC64;
     MKNAELNQRR QDATPRGVGV MCGFYAERAE NATLWDVEGN EVIDFASGIA VLNTGHRHPK
     VIAAIEKQLK AFTHTAYQIV PYESYVTLAE RINQRAPIEG PCKTAFFTTG AEAVENAVKI
     ARAHTGRPGL ITFGGGFHGR TYMTMALTGK VAPYKLGFGP FPGSVFHGQY PNALYGVTTE
     DAMNSLERIF KADIDPKQVA AIVLEPVQGE GGFNIAPAEF MQALRTLCDE HGILLIADEV
     QTGFARTGKL FAMDHYSVKP DLITMAKSLA GGMPLSAVAG RAEVMDAPAP GGLGGTYAGN
     PLAVAAALAV LEVIEEEQLC QRSQRLGQHL VEVLQQARQT SKAIVDIRAQ GSMVAVEFND
     PATGKPSAEI TRQVQQKALA EGLLLLSCGV NGNVIRFLYP LTIPEDQFTK ALGILSRALA
     Q
//