ID G8RIN5_MYCRN Unreviewed; 446 AA.
AC G8RIN5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEV75942.1};
GN OrderedLocusNames=MycrhN_5469 {ECO:0000313|EMBL:AEV75942.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75942.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV75942.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV75942.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) 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; CP003169; AEV75942.1; -; Genomic_DNA.
DR RefSeq; WP_014213681.1; NC_016604.1.
DR AlphaFoldDB; G8RIN5; -.
DR STRING; 710685.MycrhN_5469; -.
DR KEGG; mrh:MycrhN_5469; -.
DR PATRIC; fig|710685.3.peg.5493; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000005442; 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:AEV75942.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW Transferase {ECO:0000313|EMBL:AEV75942.1}.
SQ SEQUENCE 446 AA; 47074 MW; B0E49E770E18CBE1 CRC64;
MSTLEQSRYL ATEIPGPLSK ALIDRKSAAV SRGVGNTMSV YASRAFGGIV EDVDGNRLID
LGSGIAVTTI GNSSPAVVAA VQDQVARFTH TCFMITPYEG YVAVAEQLNR LTPGSGEKRS
ALFNSGSEAV ENAIKVARTY TRKQAVVSFD HAYHGRTNLT MALTAKSMPY KHGFGPFAPE
VYRAPLSYPF RDAEFGKEMA TDGELAAKRA IAVMDKQVGA DNLAAVIIEP IQGEGGFIVP
ADGFLPALLN WCRDNNVVFI ADEVQTGFAR TGAMFACEHE GIEPDLIVTA KGIADGMPLS
GVTGRAEIMD APHVSGLGGT YGGNPVACAA ALATIETIEA DGLVERAQQI EALMKDRLGR
LQAEDDRIGD VRGRGAMIAM ELVKAGSIEP DPDLTKALCA GCHAAGVIVL SCGTFGNVLR
FLPPLTISDD LLIEGLDVLA LVLKDL
//
