ID I0JN76_HALH3 Unreviewed; 394 AA.
AC I0JN76;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=HBHAL_3251 {ECO:0000313|EMBL:CCG45596.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG45596.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG45596.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; HE717023; CCG45596.1; -; Genomic_DNA.
DR RefSeq; WP_014643487.1; NC_017668.1.
DR AlphaFoldDB; I0JN76; -.
DR STRING; 866895.HBHAL_3251; -.
DR KEGG; hhd:HBHAL_3251; -.
DR PATRIC; fig|866895.3.peg.2268; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:CCG45596.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CCG45596.1}.
FT DOMAIN 31..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 42824 MW; 031C470379A08AA2 CRC64;
MELANRVQSL TPSSTLAITA QAKALKAEGH DVIGLGAGEP DFNTPAHILD AAKRAMDEGL
TKYTPAGGIP ELKNAISAKL KRDQNLTYTN EQIIVTTGAK HALFTLFQVL LNKGDEVIVP
APYWVSYPEQ IKLAEGKPVI VTADESNNFK ITPEQLKASI SEHTKAVVIN SPSNPTGMMY
SEKELQALGQ VCLDNDILII SDEIYEKLVY TSEEHISIAQ LSEELYNQTV IINGVSKSHS
MTGWRIGFAA GNKTIIKAMS NMASHSTSNP TSIAQYAALA AYIGSDEDVT KMREAFKERL
DVLYDKLTSI PGVECVKPSG AFYLFPNVQK AAESGGFSDV DEWVKALLDQ EKVALVPGSG
FGSPQNVRLS YATSLDQLEK AADRIKQFVN NHQS
//