ID A3XIJ0_LEEBM Unreviewed; 451 AA.
AC A3XIJ0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EAQ50628.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EAQ50628.1};
GN ORFNames=MED217_06332 {ECO:0000313|EMBL:EAQ50628.1};
OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS MED217) (Flavobacterium sp. (strain MED217)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ50628.1, ECO:0000313|Proteomes:UP000001601};
RN [1] {ECO:0000313|EMBL:EAQ50628.1, ECO:0000313|Proteomes:UP000001601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ50628.1,
RC ECO:0000313|Proteomes:UP000001601};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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:EAQ50628.1}.
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DR EMBL; AANC01000002; EAQ50628.1; -; Genomic_DNA.
DR RefSeq; WP_009779650.1; NZ_CH672395.1.
DR AlphaFoldDB; A3XIJ0; -.
DR STRING; 398720.MED217_06332; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_4_0_10; -.
DR OrthoDB; 730777at2; -.
DR Proteomes; UP000001601; 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 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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 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:EAQ50628.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW Transferase {ECO:0000313|EMBL:EAQ50628.1}.
SQ SEQUENCE 451 AA; 49852 MW; 4CE2C5D80E019781 CRC64;
MKEKLSKNEM IVEGDINLSE ARKTWLKDQV STEAKTLLEK DAKYFMHQAL STPCLDVLAN
AQGALITNTS GKNYFDFHGN NVHQLGFSHP KLVAALKQQL DALTFSTRRY TNKTAINFAE
KLTSLTPGLD KILMTPNGSS AVGIALKLAR AVTGKYKVLS FWDSFHGASL DVVSVSGESV
FREQMGPMMP GVERIPPPIT YRGIYESNEE KALEYLEYIL AKDNQIGAFL AETVRNTDAQ
IPSKHFWKAA RKLCDQYGVL LILDEIPIAL GRTGKLFAYE HYDIIPDILC LGKGLGGGII
PQAAIVTKKE FDQFNQISLG HYTFEKSPMG AAAAHTTLEI IEGEHLLEHV VYLEGMMQAE
LNQLQADFEL IGDVRGIGLL WGIELVTSRV TKEKASAQAE AIMYECLKNG LSFKVSKGNV
LQLCPALTIT ETQLAEALNI LRTAFYKITQ A
//
