ID   C5CB15_MICLC            Unreviewed;       440 AA.
AC   C5CB15;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ACS30548.1, ECO:0000313|EMBL:SQG49505.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:SQG49505.1};
GN   Name=puuE {ECO:0000313|EMBL:SQG49505.1};
GN   OrderedLocusNames=Mlut_10360 {ECO:0000313|EMBL:ACS30548.1};
GN   ORFNames=NCTC2665_02056 {ECO:0000313|EMBL:SQG49505.1};
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS   NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Micrococcus.
OX   NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS30548.1, ECO:0000313|Proteomes:UP000000738};
RN   [1] {ECO:0000313|EMBL:ACS30548.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS30548.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT   "Complete sequence of Micrococcus luteus NCTC 2665.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000000738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC   NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX   PubMed=19948807; DOI=10.1128/JB.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA   Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA   Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA   Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
RN   [3] {ECO:0000313|EMBL:SQG49505.1, ECO:0000313|Proteomes:UP000248985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG49505.1,
RC   ECO:0000313|Proteomes:UP000248985};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; CP001628; ACS30548.1; -; Genomic_DNA.
DR   EMBL; LS483396; SQG49505.1; -; Genomic_DNA.
DR   RefSeq; WP_010078814.1; NZ_WBMF01000107.1.
DR   AlphaFoldDB; C5CB15; -.
DR   STRING; 465515.Mlut_10360; -.
DR   EnsemblBacteria; ACS30548; ACS30548; Mlut_10360.
DR   KEGG; mlu:Mlut_10360; -.
DR   PATRIC; fig|465515.4.peg.987; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000000738; Chromosome.
DR   Proteomes; UP000248985; Chromosome 1.
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   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:ACS30548.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW   Transferase {ECO:0000313|EMBL:SQG49505.1}.
SQ   SEQUENCE   440 AA;  46185 MW;  74A29BC777944223 CRC64;
     MTATPDLEQT RHLATELPGP RSRELAERQQ RAVPAGVATT MPVYAARAAG GILEDVDGNR
     LIDLASGIAV TSVGASHPRV VAAVQEQVAQ FTHTSFMITP YEGYVAVAEQ LDRTSPIPGE
     TRTALFNSGA EAVENAVKVA RAYTGKQAVA AFDHAYHGRT TLTMALTAKS MPYKHSFGPF
     APEIYRVPGS YPLRDGLSGA EAAQRAISAL EKQIGADDLA AVIMEPIQGE GGFIVPAEGF
     LPAMVEWCKA NDVLFIADEV QSGIARTGAW FASETEGIEP DLMATAKGIA GGMPLSGVTG
     RAEVMDSVHP GGLGGTYGGN PVATAAALAV FEAVEEDGLL EKARRIEQVI REHFEQNADD
     RIAEVRGRGA MMAIEFVDPA TGEPDATLTA TVAAAVRATG VILLTCGTYG NVVRFLPPLT
     IGEDLLKEGL SEVTKALQSA
//