ID C1D790_LARHH Unreviewed; 397 AA.
AC C1D790;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=LHK_01340 {ECO:0000313|EMBL:ACO74330.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO74330.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO74330.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO74330.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO74330.1; -; Genomic_DNA.
DR RefSeq; WP_012696816.1; NC_012559.1.
DR AlphaFoldDB; C1D790; -.
DR STRING; 557598.LHK_01340; -.
DR KEGG; lhk:LHK_01340; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_4; -.
DR Proteomes; UP000002010; 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 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:ACO74330.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ACO74330.1}.
FT DOMAIN 31..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 42801 MW; D8DF526E9BA30765 CRC64;
MELSHRVNAI KESPTLAITA KAQKLKAEGR DVVALAAGEP DFDTPDHIKA AAIEAINKGF
TKYTPVSGTP ALKKAIVEKF KRDNGLEYAA NQVLVSVGGK QSFYNLCQAY INDGDEVIIP
APYWVSYPDM TILAGGVPVV VECGIEQGYK LSPAQLEAAI TPKTRMLVIN SPSNPTGAVY
TLEELKALGD VLKKHPNILV ASDDMYEHVM LGDTKFYNIL NACPELKEQV IVLNGVSKAY
SMTGWRIGYA AGPQKLIKAM ENIQSQSTSN PTSISQVAAQ AALEGDQGCI TPMLKAFNER
HVYVVDRFNK MRGLKCLRAG GAFYAFVDAR EAIKLLAAEG KIAGATDMAL GTYLLEAQDV
AVVPGSAFGA EGYFRISFAT SMQNLEKALD RIEKALA
//
