ID E7ACF7_HELFC Unreviewed; 437 AA.
AC E7ACF7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375,
GN ECO:0000313|EMBL:CBY82186.1};
GN OrderedLocusNames=Hfelis_01020 {ECO:0000313|EMBL:CBY82186.1};
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY82186.1, ECO:0000313|Proteomes:UP000007934};
RN [1] {ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBY82186.1, ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RX PubMed=21402865;
RA Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G.,
RA Falkow S., Bentley S.D., Muller A.;
RT "Comparative whole genome sequence analysis of the carcinogenic bacterial
RT model pathogen Helicobacter felis.";
RL Genome Biol. Evol. 3:302-308(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC EC=5.4.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00375};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00375};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004819, ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
CC {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
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DR EMBL; FQ670179; CBY82186.1; -; Genomic_DNA.
DR RefSeq; WP_013468556.1; NC_014810.2.
DR AlphaFoldDB; E7ACF7; -.
DR STRING; 936155.HFELIS_01020; -.
DR GeneID; 36134868; -.
DR KEGG; hfe:HFELIS_01020; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_7; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000007934; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_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 HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00713; hemL; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBY82186.1};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00375};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00375}; Reference proteome {ECO:0000313|Proteomes:UP000007934};
KW Transferase {ECO:0000313|EMBL:CBY82186.1}.
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 437 AA; 46768 MW; 8075ACB9AEF44B8D CRC64;
MAKKQLGHAL LHSINDFNEA KQVIAGGVNS PVRAFKSVGG TPPFIFKGDG YSLYDVDGNS
YVDFVQSWGP LLFGHADAQI QERVIEVLKR GMSFGAPTEL ETTLAKKLVL SYEGVEKVRL
VSSGTEATMS AIRLARAFSG KDRIIKFEGC YHGHSDSLLV DAGSGCATFG VPSSLGVPKA
ISDQTLIAQY NDIDSVKACF EAGGVGCVII EPIAGNMGLV PAKLEFLQEL QHLCNKYEAV
LIFDEVMSGF RAGVNGSQTH HRLVPDLVTF GKVIGGGLPL ACFGGRAEIM EMLAPVGGVY
QAGTLSGNPV AVAAGIVALE KIAQEPKLFS RLEELAQRFV KGLVKIAASH GIALQGCVRG
SMFGFFFSEQ EVQDFQGAKN SKTDLYARLH QKMLQRGVYL APSAFETGFI CAPMHVDIID
ACLQKAQESF SEIAHGI
//
