ID A0A0F5PEV1_9SPHN Unreviewed; 432 AA.
AC A0A0F5PEV1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KKC26114.1};
GN ORFNames=WP12_10670 {ECO:0000313|EMBL:KKC26114.1};
OS Sphingomonas sp. SRS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC26114.1, ECO:0000313|Proteomes:UP000033680};
RN [1] {ECO:0000313|EMBL:KKC26114.1, ECO:0000313|Proteomes:UP000033680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC26114.1,
RC ECO:0000313|Proteomes:UP000033680};
RA Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT isolated from an agricultural field in the United Kingdom.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKC26114.1}.
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DR EMBL; LARW01000084; KKC26114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F5PEV1; -.
DR STRING; 133190.WP12_10670; -.
DR PATRIC; fig|133190.4.peg.4017; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000033680; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:KKC26114.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000033680};
KW Transferase {ECO:0000313|EMBL:KKC26114.1}.
SQ SEQUENCE 432 AA; 45643 MW; 55CBA9B497E6419A CRC64;
MVNAFTGDPS SLAPVTRQLI ERRARLLGPA YRLFYEQPLH LVRGDGVWLY DADDQPYLDV
YNNVASIGHC HPRVVEAIQR QVATLNTHTR YLHETILDYA ERLLATFPPE LSQVLFTCTG
SEANDLALRI AEAATGGTGV IVTELAYHGL THAVSGMSPS LGAHVPRGPH VWTVPAPRDA
RDIEDVGAGF AAGVAAALAE MQSQGVRPAA LFCDTIFSSD GIFSDPPGFL IEAVDAVRAA
GGLFIADEVQ PGFGRTGQAM WGFARHSVVP DMVSLGKPMG NGHPIAGLVV RPDIVAEFGA
NARYFNTFGG NPVSCAAGLA TLSAIEEYGL VARAHSVGTY LREGLSALAG RDGRIAAVRG
VGLFVGVELG EGGLPDPALT GRIVNGLRER RVLISATGPS ANVLKIRPPL VFGREHVDLL
LAALTAELDG AH
//
