ID   Q2LW66_SYNAS            Unreviewed;       447 AA.
AC   Q2LW66;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABC78326.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABC78326.1};
GN   ORFNames=SYN_01215 {ECO:0000313|EMBL:ABC78326.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78326.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC78326.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC78326.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC78326.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LW66; -.
DR   STRING; 56780.SYN_01215; -.
DR   KEGG; sat:SYN_01215; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_7; -.
DR   InParanoid; Q2LW66; -.
DR   Proteomes; UP000001933; 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   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:ABC78326.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933};
KW   Transferase {ECO:0000313|EMBL:ABC78326.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  49113 MW;  6C12244006FB7173 CRC64;
     MIMKENGNSC SGTRMSKEGE TMREDLVTRT QRLLAPSLVI HSDIVVKRGH GVYLESVDGK
     RYLDFTSGLA VANVGHSHPK IVEAIKKQAE ELVHAGCMFY YEPLAEYPER LKEVTPPGLD
     RFFFSNSGAE AIEGALKLAR YFTGRQGILA FSGAFHGRTY GALSLTASNA KYRNRYAPLL
     PSVYHAPYPY CYRCDIGREP ETCSLECFGH VETLLNRLIA PEEIACAVIE PMLGEGGYVV
     PPARYLKKLR KLCDREGILL IFDEVQSGMG RTGRWFASEH FGIVPDIMTL AKGIANGMPL
     SAVVSSGRIM DGWAPGTHGT TFGGNPVSLC AAAATLRVIE EERLLENAAV VGSKALERLE
     SMKDRHPVIG DVRGRGLMIG VEFVREGKEP DRATVEKIMK TCLDRGLLLV ECGGDKNILR
     LIPPLVITRE EMDHGLDILE EAIVKSA
//