ID A0A0A7I6W9_9BIFI Unreviewed; 454 AA.
AC A0A0A7I6W9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AIZ15968.1};
GN ORFNames=AH67_02685 {ECO:0000313|EMBL:AIZ15968.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ15968.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ15968.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ15968.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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; CP007457; AIZ15968.1; -; Genomic_DNA.
DR RefSeq; WP_039171355.1; NZ_CP007457.1.
DR AlphaFoldDB; A0A0A7I6W9; -.
DR STRING; 1447715.AH67_02685; -.
DR KEGG; bpsp:AH67_02685; -.
DR HOGENOM; CLU_016922_8_0_11; -.
DR OrthoDB; 3246809at2; -.
DR Proteomes; UP000030636; Chromosome.
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:AIZ15968.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000030636};
KW Transferase {ECO:0000313|EMBL:AIZ15968.1}.
SQ SEQUENCE 454 AA; 49240 MW; DE4AA95002E0F9D8 CRC64;
MATRSTIMDT NSFRPEMAAA LDPETRRLTE ERDVLGPAYR LFYRTPVHLV KGEGAHVWDA
DGTEYLDVYN NVASVGHAHP RVVEAIARQA SLLNTHTRYL HENILKYADD ILSTMPDELN
RIMFQCTGSE ANDLAVRVAQ AYTGGEGVIV TAEAYHGNSA LTSKLSPALG TAQDLGLTMR
MIPTPDTYRL VIDGKPASAC TAEEFGGWMA AEVRKAVADM NRHGIKFAAL LADSIFSSDG
VYPDPVGYLQ PVIDTVHELG GVWIADEVQP GFTRTGDAFW GFERQEIVPD LVTSGKPMAN
GLPTSLMAAR QEVLEPFAGS IPYFNTFGGN PVCMAAAQAT LDVMCSEDTM GNAKRVGAIF
KQAVTDLMPA HPCIGDVRGA GLYIGCEIVK PGTKDPDQAA ALDILETLRA HHVLTSVCGR
FGNILKLRPP LVFSEQDVDW FMSAFTDTLQ ELGL
//
