ID V8CKK3_9HELI Unreviewed; 391 AA.
AC V8CKK3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF2087_00818 {ECO:0000313|EMBL:ETD27894.1};
OS Helicobacter canis NCTC 12740.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357399 {ECO:0000313|EMBL:ETD27894.1, ECO:0000313|Proteomes:UP000018688};
RN [1] {ECO:0000313|EMBL:ETD27894.1, ECO:0000313|Proteomes:UP000018688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12740 {ECO:0000313|EMBL:ETD27894.1,
RC ECO:0000313|Proteomes:UP000018688};
RG The Broad Institute Genomics Platform;
RA Earl A., Fox J.G., Shen Z., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Helicobacter canis NCTC 12740.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETD27894.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZJJ01000001; ETD27894.1; -; Genomic_DNA.
DR RefSeq; WP_023929750.1; NZ_KI669458.1.
DR AlphaFoldDB; V8CKK3; -.
DR STRING; 1357399.HMPREF2087_00818; -.
DR PATRIC; fig|1357399.3.peg.862; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_2_7; -.
DR OrthoDB; 5362312at2; -.
DR Proteomes; UP000018688; Unassembled WGS sequence.
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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000018688};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 75..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 391 AA; 44005 MW; 85DADB150E8916E6 CRC64;
MIHLNANDLA LTHSLAKLKA ASGSHSPSIA TLRETLPALK IKIDACFLSN PYATDLFMQE
LESKLIAQGG LRDALEFYPS QNAAIAQKLA KYLHIDSSHI FIGNGAIEVI QAVLHNFVRT
NLVVPIPTFS SYYEFVRDGV EVLLYKLPKE QNYALDIEAY TKFIQDHNAK NALIINPNNP
DGGYIPYDTL RECLARLRHL ESVIIDESFL HFGYEDSSLE QISYTKLVEE FSNVVLIKSM
SKDFGVAGLR AGYGVMAKNR VEALLHNGYL WNVNGLSEFF FSLFGDDEFL QKYERVRKSY
ITQTQEFFKA LGQIDSIKTY PSKANFALVE LLNGAKAQDL CIKLLSSYGI YTRSCSDKIG
LEGEFLRIAS RSEQENTQIL QSLQEIFTGD F
//
