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Database: UniProt/TrEMBL
Entry: E1PZD4_HELPM
LinkDB: E1PZD4_HELPM
Original site: E1PZD4_HELPM 
ID   E1PZD4_HELPM            Unreviewed;       390 AA.
AC   E1PZD4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=HPSJM_03415 {ECO:0000313|EMBL:ADO02275.1};
OS   Helicobacter pylori (strain SJM180).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=765962 {ECO:0000313|EMBL:ADO02275.1, ECO:0000313|Proteomes:UP000006862};
RN   [1] {ECO:0000313|Proteomes:UP000006862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJM180 {ECO:0000313|Proteomes:UP000006862};
RA   Kersulyte D., Velapatino B., Gilman R.H., Berg D.E.;
RT   "Complete genome sequence of Helicobacter pylori strain SJM180.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002073; ADO02275.1; -; Genomic_DNA.
DR   RefSeq; WP_000967353.1; NC_014560.1.
DR   AlphaFoldDB; E1PZD4; -.
DR   KEGG; hpm:HPSJM_03415; -.
DR   HOGENOM; CLU_017584_4_3_7; -.
DR   Proteomes; UP000006862; 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:ADO02275.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ADO02275.1}.
FT   DOMAIN          30..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   390 AA;  42877 MW;  366C153AE917D53F CRC64;
     MLYSSKIQSL SESTTIAIST LAKELKSQGK DILSFSAGEP DFDTPQAIKD AAIKALNEGF
     TKYTPVAGIP ELLKAIAFKL KKENNLDYEL SEILVSNGAK QSLFNAIQAL IEKGDEVVIP
     VPFWVTYPEL VKYSGGVSQF IQTDEKSHFK ITPKQLKDAL SPKTKMLILT TPSNPTGMLY
     SKAELEALGE VLKETKVWVL SDEIYEKLVY KGEFVSCAAV SEEMKKRTIT INGLSKSVAM
     TGWRMGYAAS KDKKLVKLMN NLQSQCTSNI NSITQMASIV ALEGLVDKEI ETMRQAFEKR
     CNLAHAKINA IGGLNALKPD GAFYLFIHIG SLCGGDSMRF CHELLEKEGV ALVPGKAFGL
     EGYVRLSFAC SEEQIEKGIE RIARFVKSKG
//
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