ID F7XP43_METZD Unreviewed; 425 AA.
AC F7XP43;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=Mzhil_1496 {ECO:0000313|EMBL:AEH61335.1};
OS Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS (Methanohalophilus zhilinae).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH61335.1, ECO:0000313|Proteomes:UP000006622};
RN [1] {ECO:0000313|EMBL:AEH61335.1, ECO:0000313|Proteomes:UP000006622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5
RC {ECO:0000313|Proteomes:UP000006622};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL Submitted (JUL-2010) 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|ARBA:ARBA00001579,
CC 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 -!- 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; CP002101; AEH61335.1; -; Genomic_DNA.
DR RefSeq; WP_013898772.1; NC_015676.1.
DR AlphaFoldDB; F7XP43; -.
DR STRING; 679901.Mzhil_1496; -.
DR GeneID; 10823133; -.
DR KEGG; mzh:Mzhil_1496; -.
DR HOGENOM; CLU_016922_1_5_2; -.
DR OrthoDB; 6524at2157; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000006622; 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:InterPro.
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 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:UP000006622}.
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 425 AA; 46593 MW; 9877443BC14EEADC CRC64;
MNLKKSEELY QKAKDVLPGG VSSPVRAIKP YPFYTDSAYG SKIKDIDGNE YIDYCMGYGP
NIFGHSNPII RKAIVDQLNK GWLFGTPIEN EFKLADKITD YYPSIDMLRF VSTGTEATMS
ALRTARGFTG KNKFIKIEGG FHGAHDSVLV KAGSGATTLG KPDSLGVPEK STAHTLQVPF
NDIESMTEIV ESHKDDLAAV IMEPVMGNIG PILPHKGYLS EVRKLTQEND IVLIFDEVIT
GFRLSMGGAQ EYYGITPDMT TLGKVIGGGL PIGVFGGKRE IMEMVSPSGD IYQAGTFSGS
PSVMAAGLAV IEQLEKENIH KKLNSRGDEL RSGLRDIVDD TGLDYSVSGI ASMFKIFFGD
SPANYQDSLK CDKSEYVQFF RRMLENGIFL PPSQFETNFL STAHTDSDIE KTIRAYESNL
KGSLE
//
