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Database: UniProt/TrEMBL
Entry: V5XD62_MYCNE
LinkDB: V5XD62_MYCNE
Original site: V5XD62_MYCNE 
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
//
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