ID   A1T889_MYCVP            Unreviewed;       446 AA.
AC   A1T889;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABM13389.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABM13389.1};
GN   OrderedLocusNames=Mvan_2581 {ECO:0000313|EMBL:ABM13389.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM13389.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM13389.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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; CP000511; ABM13389.1; -; Genomic_DNA.
DR   RefSeq; WP_011779798.1; NZ_JACKSD010000179.1.
DR   AlphaFoldDB; A1T889; -.
DR   STRING; 350058.Mvan_2581; -.
DR   KEGG; mva:Mvan_2581; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000009159; 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   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:ABM13389.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Transferase {ECO:0000313|EMBL:ABM13389.1}.
SQ   SEQUENCE   446 AA;  47153 MW;  C24E466B1AEBBC84 CRC64;
     MSALEQSRHL ATAIPGPRSC ELIARKSAAV ARGVGTTMPV YAARAFGGIV EDVDGNRLID
     LGSGIAVTTI GNASPKVVER AAEQLHKFTH TCFMVTPYEG YVAVAEALNR LTPGDGDKRT
     ALFNSGSEAV ENAVKIARSY TRKQAVVSFD HAYHGRTNLT MALTAKSMPY KHGFGPFAPE
     IYRAPLSYPF RDAEFGKELA TDGELAARRA ITVIDKQVGA DNLAAVIIEP IQGEGGFIVP
     AEGFLPTLLE WCHANGVVFI ADEVQTGFAR TGAMFACEHE GIVPDLIVTA KGIADGMPLS
     AVTGRAEIMD APHVSGLGGT YGGNPVACAA ALATIETIES DGLVARAAQI ETLMKDKLGR
     LQAEDDRIGD VRGRGAMIAV ELVKPGTLEP DPELTKNLLA AAHRAGVIVL SCGTFGNVLR
     FLPPLAISDE LLLEGLDVLE LILRDL
//