ID   Q1CTK0_HELPH            Unreviewed;       390 AA.
AC   Q1CTK0;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=HPAG1_0655 {ECO:0000313|EMBL:ABF84722.1};
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544 {ECO:0000313|EMBL:ABF84722.1, ECO:0000313|Proteomes:UP000008835};
RN   [1] {ECO:0000313|EMBL:ABF84722.1, ECO:0000313|Proteomes:UP000008835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1 {ECO:0000313|EMBL:ABF84722.1,
RC   ECO:0000313|Proteomes:UP000008835};
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84722.1; -; Genomic_DNA.
DR   RefSeq; WP_000967349.1; NC_008086.1.
DR   AlphaFoldDB; Q1CTK0; -.
DR   KEGG; hpa:HPAG1_0655; -.
DR   HOGENOM; CLU_017584_4_3_7; -.
DR   Proteomes; UP000008835; 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:ABF84722.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABF84722.1}.
FT   DOMAIN          30..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   390 AA;  42914 MW;  F1BD674E1CC90DE9 CRC64;
     MLYSSKIQSL SESTTIAIST LAKELKSQGK DILSFSAGEP DFDTPQAIKD AAIKALNDGF
     TKYTPVAGIP ELLKAIAFKL KKENSLDYEP NEILVSNGAK QSLFNAIQAL IGEGDEVIIP
     VPFWVTYPEL VKYSNGVSKF IQTDEKSRFK ITPKQLKNAL SPKTKMLILT TPSNPTGMLY
     SKAELEALGE VLKDTKIWVL SDEIYEKLVY KGEFVSCAAV SEEMKKRTIT INGLSKSVAM
     TGWRMGYAAS KDKKLVKLMN NLQSQCTSNI NSITQMASIV ALEGLVDKEI ETMRQAFEKR
     CDLAHAKINA IKGLNALKPD GAFYLFINIG SLCGGDSMRF CHELLEKEGV ALVPGKAFGL
     EGYVRLSFAC SEEQIEKGIE RIARFVKSKG
//