ID   C4XSR3_SOLM1            Unreviewed;       441 AA.
AC   C4XSR3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAH75755.1};
GN   Name=gabT {ECO:0000313|EMBL:BAH75755.1};
GN   OrderedLocusNames=DMR_22640 {ECO:0000313|EMBL:BAH75755.1};
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370 {ECO:0000313|EMBL:BAH75755.1, ECO:0000313|Proteomes:UP000009071};
RN   [1] {ECO:0000313|EMBL:BAH75755.1, ECO:0000313|Proteomes:UP000009071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1
RC   {ECO:0000313|Proteomes:UP000009071};
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP010904; BAH75755.1; -; Genomic_DNA.
DR   RefSeq; WP_015860937.1; NC_012796.1.
DR   AlphaFoldDB; C4XSR3; -.
DR   STRING; 573370.DMR_22640; -.
DR   KEGG; dma:DMR_22640; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_7; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000009071; 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; 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:BAH75755.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:BAH75755.1}.
SQ   SEQUENCE   441 AA;  47550 MW;  61774EB86FBFD80C CRC64;
     MNTTDKAQEL QALRDRYVPK GHPNATPFFV ESAKGALLRD VTGREFIDFV GGIGVLNVGH
     CHPKVVAAVK DQAGRYLHTC SMVTMYEPYV QLAARLSEAA PGDFEKKAMF VNSGSEAVEN
     AVKIARCHTG RAGVVSMKNA FHGRTLLAMS LTSKVKPYKF GFGPLAPEVY QYPNYAYCYR
     CPLGLTYPKC GVACADKLRE FFIATAAAEN IACIIAEPVQ GEGGFVVPPK EFFEKLRAIC
     DEYGIVFIAD EIQSGFGRTS KLFAMEHFGV APDLMTVAKS MGGGLPLAGV VGKAEIMDAV
     APGGIGGTYG GNPLACRAGL AVMDIFEQDN LLAKAERLGN VVKRRFAAFK KQYQLIGDER
     GLGAMRALEF VSDRATKAPC PEAAKGVAKF CQDNGLLVLS CGNFGNCIRV LMPLVITRDQ
     LDRGLDIMEE GIREVSKSLG K
//