UniProt: A0A0A3ANX9

Database: UniProt
Entry: A0A0A3ANX9_9PAST

LinkDB:  A0A0A3ANX9_9PAST 
Original site:  A0A0A3ANX9_9PAST

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0A3ANX9_9PAST        Unreviewed;       430 AA.
AC   A0A0A3ANX9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ORFNames=OA57_11215 {ECO:0000313|EMBL:KGQ69492.1};
OS   Chelonobacter oris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Chelonobacter.
OX   NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ69492.1, ECO:0000313|Proteomes:UP000030380};
RN   [1] {ECO:0000313|EMBL:KGQ69492.1, ECO:0000313|Proteomes:UP000030380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1662 {ECO:0000313|EMBL:KGQ69492.1,
RC   ECO:0000313|Proteomes:UP000030380};
RA   Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT   "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT   respiratory disease in Hermann's Tortoises.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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}.
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:KGQ69492.1}.
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DR   EMBL; JSUM01000019; KGQ69492.1; -; Genomic_DNA.
DR   RefSeq; WP_034617888.1; NZ_JSUM01000019.1.
DR   AlphaFoldDB; A0A0A3ANX9; -.
DR   STRING; 505317.OA57_11215; -.
DR   OrthoDB; 9801052at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000030380; Unassembled WGS sequence.
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:KGQ69492.1};
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:UP000030380};
KW   Transferase {ECO:0000313|EMBL:KGQ69492.1}.
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   430 AA;  46279 MW;  942BCD2C6546028D CRC64;
     MNHSEQLFQQ AQDIIPGGVN SPVRAFKGVG GTPLFIERAD GAYIYDSDGK QYIDYVGSWG
     PMILGHNHPA IRNAVIETAQ KGLSFGAPTA LEIELAQLVC KLMPSIEMVR MVSSGTEATM
     SAIRLARGYT KRDKIIKFEG CYHGHADALL VKAGSGALTL GQPSSPGVPA DFTKHTLVCQ
     YNDPDSVKQV FEQYPQDIAC IIIEPVAGNM NCVPPKAGFL QELRTLCDQY GALLIIDEVM
     TGFRVALGGA QAHYQVTPDL TCLGKVIGGG MPVGAFGGKK SIMQHLAPLG PVYQAGTLSG
     NPIAMAAGLA CLTELSKCGN EQKLAQLTKR LAEGLKQRAA RHNIPLIVNY VGAMFGIYFT
     EQAEVSSYQQ VMACDGERFK QFFHAMLKKG VYLAPSAFEA GFMSLAHSEA DIEKTLDAAE
     TCFAEFNRIS
//

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