ID A0A0A0BTT7_9CELL Unreviewed; 475 AA.
AC A0A0A0BTT7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KGM11331.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KGM11331.1};
GN ORFNames=N868_10895 {ECO:0000313|EMBL:KGM11331.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM11331.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM11331.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11331.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM11331.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11331.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM11331.1}.
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DR EMBL; AXCY01000024; KGM11331.1; -; Genomic_DNA.
DR RefSeq; WP_052426077.1; NZ_AXCY01000024.1.
DR AlphaFoldDB; A0A0A0BTT7; -.
DR OrthoDB; 3246809at2; -.
DR Proteomes; UP000029839; Unassembled WGS sequence.
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:KGM11331.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029839};
KW Transferase {ECO:0000313|EMBL:KGM11331.1}.
FT REGION 452..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 49222 MW; 8378E36190D09D32 CRC64;
MIDVSSRLPL VRPDLPQRRL LRTAVPGPRS QEVARRRAAV VAAGVASTLP VYVERAGGGV
LVDVDGNSFV DLGSGIAVTS VGNAAPAVSA AVQEQVERTT HTCFMVAPYE EYVAVCEALA
RLTPGDHAKR SVLLNSGAEA VENAVKIARR ATGRDAVVVL DHAYHGRTNL TMAMTAKAMP
YKTGFGPFAG EVYRVPASYP LREPVPITGE EAARRATAVI EKQVGADQVA CVVVEPVQGE
GGFVVPAPGF LPALAAWCRE HGVLLVADEI QTGFARTGAM FACDHEGVVP DLVTTAKGIA
GGLPLAAVTG RAEIMDAVHP GGLGGTYGGN PAACAAALAA IDLYEHADLV GAARRIEARV
VPRLRAVAER APQVAEVRGR GAMLALELVR PGSLEPDAAE AARVARECAQ HGVLVLTCGT
YGNVLRLLPP LVIGDELLDE ALDVLEAVLE GRTPPPAARA DDAPERAVGA SGPPA
//