ID E1V5R2_HALED Unreviewed; 447 AA.
AC E1V5R2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Beta alanine--pyruvate aminotransferase {ECO:0000313|EMBL:CBV41174.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:CBV41174.1};
GN OrderedLocusNames=HELO_1291 {ECO:0000313|EMBL:CBV41174.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV41174.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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|RuleBase:RU003560}.
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DR EMBL; FN869568; CBV41174.1; -; Genomic_DNA.
DR RefSeq; WP_013331046.1; NC_014532.2.
DR AlphaFoldDB; E1V5R2; -.
DR STRING; 768066.HELO_1291; -.
DR KEGG; hel:HELO_1291; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_6; -.
DR OrthoDB; 7052035at2; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0016223; F:beta-alanine-pyruvate 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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE 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:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:CBV41174.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBV41174.1}.
SQ SEQUENCE 447 AA; 48873 MW; E2B91E856D617A75 CRC64;
MSDQNRARAA GLSPEQLDAY WMPYTGNRQF KRDPRIIVGA EGSYLKDAEG RRIYDGLSGL
WTCGAGHCRP EITEAVSRQL GELDYSPAFQ FGHPKAFELA HRLSELTPAG LNHVFFTGSG
SESADTSLKI ARAYWRKKGK PAKTKLIGRS KGYHGVNFGG ISLGGIGANR VLFGQGVDAD
HLPHTLLKEN AFTRGMPERG ADQADELLEL IALHDASNIA AVIVEPLAGS AGVIPPPKGY
LQRLREICDQ HDILLIFDEV ITGFGRMGSM TGAEEFGVVP DIINVAKQLT NGAVPMGGVI
VRDEIYQTFM EQGGPDYMLE LPHGYTYSGH PVACAAALAA LDVLENDRLI ERVREMSPVF
EEALHGLKGS RYVSDIRNYG LAGALQIEPY PGEPARRPFE IAMKCWEKGF YVRYGGDTIQ
LGLPFIVERE EIDRLINALG DALGELD
//
