ID E1V508_HALED Unreviewed; 470 AA.
AC E1V508;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:CBV41057.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CBV41057.1};
GN OrderedLocusNames=HELO_1174 {ECO:0000313|EMBL:CBV41057.1};
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:CBV41057.1, 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|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FN869568; CBV41057.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V508; -.
DR STRING; 768066.HELO_1174; -.
DR KEGG; hel:HELO_1174; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_1_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000008707; 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; 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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBV41057.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBV41057.1}.
SQ SEQUENCE 470 AA; 52710 MW; 59947A55A83FC120 CRC64;
MSNIPDVSHF SSLDNKRLIE SDKAHYMHGY HAFDEHRQHG SLNITQGDDA YIRDAQGQQY
LDAVGGMWCT NIGLAREEMA QAIAEQTRQL AYSNSFCDMA NDRAIQLSEK LAELAPGDLD
RVFLTTGGST AVDTAIRLVH YYQNCRGKHE KKQIITRINA YHGSTYLTMS LGGKQADRPE
EFDFLTDGIH HLSCPNFYRA PEGVNEAEFL EGLVAEFENK ILEIGPERVG AFLAEPIMGS
GGVIIPPAGY HRRMWEVCQR HDVLYISDEV VTSFGRLGHF FASEAEFDIQ PDIITTAKGL
TSGYQPLGAC IFSERIWEVI AEPGAGRCFS HGFTYSGHPV ACAAALKNIE ILEREALLPR
AREVGRYFEQ RLRTLEDLPI VGEVRARCFM ACVEFVADKT TRTLFPEALN IGEWVHLRAQ
KRGLLVRPIV HLNVMSPALT LTHEQVDFVV DVLRESILET LEDLRAAGHW
//
