UniProt: A8V0S0

Database: UniProt
Entry: A8V0S0_9AQUI

LinkDB:  A8V0S0_9AQUI 
Original site:  A8V0S0_9AQUI

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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   A8V0S0_9AQUI            Unreviewed;       428 AA.
AC   A8V0S0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=HG1285_04066 {ECO:0000313|EMBL:EDP73982.1};
OS   Hydrogenivirga sp. 128-5-R1-1.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX   NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP73982.1, ECO:0000313|Proteomes:UP000005981};
RN   [1] {ECO:0000313|EMBL:EDP73982.1, ECO:0000313|Proteomes:UP000005981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP73982.1,
RC   ECO:0000313|Proteomes:UP000005981};
RA   Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP73982.1}.
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DR   EMBL; ABHJ01000101; EDP73982.1; -; Genomic_DNA.
DR   RefSeq; WP_008288556.1; NZ_ABHJ01000101.1.
DR   AlphaFoldDB; A8V0S0; -.
DR   PATRIC; fig|392423.7.peg.1132; -.
DR   OrthoDB; 9807885at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000005981; 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:EDP73982.1};
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:UP000005981};
KW   Transferase {ECO:0000313|EMBL:EDP73982.1}.
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   428 AA;  46667 MW;  9A14158BC47F9222 CRC64;
     MGFEKSKKLF EEAQKYLVGG VNSPVRAFKA LGGTPIFIEK AKGSRVWDVD GNEYIDYVLS
     WGPLILGHAN DQIINAIKQV SNYGTSFGAP TELEVEMAKA VVEAVPSIEM LRFVNSGTEA
     TMSAIRLARG YTGKKKIIKF DGCYHGHGDS LLVSAGSGVA TLGIPGTPGI PEELASLTIV
     LPYNDIEAVE EAFKKHGDDI ACVIIEPVAG NMGVVAPPKE YHQRLREITK EYGSLLIWDE
     VMTGFRLALG GAQELYGIDP DLTTLGKVIG AGLPVGAYGG KAEIMKHVAP EGPVYQAGTL
     SGNPLAMAAG LRQLQILKEK NPYPELDKKG EKLEKGLKDL IIKYSIKATV NRVGSMITMF
     FTDKEVKNFQ DAKSSDLEMF NKFFWKMIEK GVYLAPSQFE ASFLSTAHSE EDINRTLEAV
     EETFKELT
//

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