ID V5XD62_MYCNE Unreviewed; 447 AA.
AC V5XD62;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AHC25359.1};
GN ORFNames=D174_12545 {ECO:0000313|EMBL:AHC25359.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC25359.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC25359.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC25359.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
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; CP006936; AHC25359.1; -; Genomic_DNA.
DR RefSeq; WP_019511278.1; NC_023036.2.
DR AlphaFoldDB; V5XD62; -.
DR KEGG; mne:D174_12545; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR Proteomes; UP000018763; 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; 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; ORNITHINE AMINOTRANSFERASE; 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:AHC25359.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018763};
KW Transferase {ECO:0000313|EMBL:AHC25359.1}.
SQ SEQUENCE 447 AA; 46915 MW; 67C9FE29D6D2AF1C CRC64;
MPAVEQSRHL ATAIPGPKSS ALIERKNSAV ARGVGTTMPV YAARAAGGIL EDIDGNRLID
LGSGIAVTTI GNAAPRVVDA VTAQVDLFTH TCFMVTPYEG YVAVAEHLNR LTPGSGDKRS
ALFNTGSEAV ENAIKIARSY TRKQAVVSFD HAYHGRTNLT MALTAKSMPY KSGFGPFAPE
IYRAPLSYPF RDAEFGKELA EDGELAAKRA ITVIDKQIGA DNLAAVIIEP IQGEGGFIVP
APGFLPALLA WCRDNNVVFI ADEVQTGFAR TGAMFACEHE GIEPDLIVTA KGIADGLPLS
AVTGRAEIMD APHVSGLGGT YGGNPIACAA ALATIETIET DGLVARAGAI ERLMKDRLHR
MQADDDRIGD VRGRGAMIAV ELVKSGGTEP DADLTKALCA AAHAKGVIVL SCGTYGNVLR
FLPPLAISDD LLNEALEILA EALAALR
//