ID   A0M3E3_CHRFK            Unreviewed;       435 AA.
AC   A0M3E3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CAL67138.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CAL67138.1};
GN   Name=gabT {ECO:0000313|EMBL:CAL67138.1};
GN   OrderedLocusNames=GFO_2173 {ECO:0000313|EMBL:CAL67138.1};
OS   Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS   (Gramella forsetii).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=411154 {ECO:0000313|EMBL:CAL67138.1, ECO:0000313|Proteomes:UP000000755};
RN   [1] {ECO:0000313|EMBL:CAL67138.1, ECO:0000313|Proteomes:UP000000755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803 {ECO:0000313|EMBL:CAL67138.1,
RC   ECO:0000313|Proteomes:UP000000755};
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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|RuleBase:RU003560}.
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DR   EMBL; CU207366; CAL67138.1; -; Genomic_DNA.
DR   RefSeq; WP_011710041.1; NC_008571.1.
DR   AlphaFoldDB; A0M3E3; -.
DR   STRING; 411154.GFO_2173; -.
DR   KEGG; gfo:GFO_2173; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_10; -.
DR   OrthoDB; 730777at2; -.
DR   Proteomes; UP000000755; 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   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; 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   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:0000313|EMBL:CAL67138.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CAL67138.1}.
SQ   SEQUENCE   435 AA;  47422 MW;  3C7576AEF74555F3 CRC64;
     MIEKNTQAQE LLERRKNIVA NGVGIFNTAT VKEAKGAIIT DVDGRELIDF AGGIGVVNAG
     HCPEPVVEAI REQAGKYLHT SFNVVTYEPY IKLCEELAEI LPHGEKTKAM LISTGAEAVE
     NAIKIARQAT KRPAILCYTE AYHGRTLMAM SLTSKVNYKF SSGPFAPEVY RIPFPNFYKY
     GGTQEMDDFV DTELNRLRES AHSMVDINSV AAIIIEPIQG EGGFNPVPQR YLEGLRSFCD
     EHGVLLILDE IQSGFCRTGH WASWQHYNVE PDISTYAKSL GSGLPIAAVL GKAEIMDAAG
     SGTIGGTYIG SPVCCAAALA TIQYMKDINL NERAVQVGKI VTDRIKKLQK EYPGIGDVRG
     IGAMIGIEFV KENNPGKPDT ELCDKIVKGC AEEGLILLSA GTFKNVIRIL SPLVITDEQL
     NKGLDILVNQ IKKNI
//