ID I4D540_DESAJ Unreviewed; 429 AA.
AC I4D540;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Desaci_1937 {ECO:0000313|EMBL:AFM40914.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM40914.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM40914.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
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; CP003639; AFM40914.1; -; Genomic_DNA.
DR RefSeq; WP_014826920.1; NC_018068.1.
DR AlphaFoldDB; I4D540; -.
DR STRING; 646529.Desaci_1937; -.
DR KEGG; dai:Desaci_1937; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000002892; 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}.
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 429 AA; 46251 MW; 9D4422DAC7A3CEF0 CRC64;
MPFVDEKSSQ AFAKAKRVIP GGVNSPVRAF KSVGRDPVFI DRAEGAYLWD IDGNRYVDYV
GSWGPLIVGH AHPEVVEAIK RVAERGTSYG APTEVETELA EEVLKAYPSM EMIRMVNSGT
EATMSALRLA RGVTGRTKIV KFEGCYHGHA DQLLIKAGSG ALTFGVPTSP GVPPQTAATT
ISARYNDLEG LREIFQREGE DIAGVILEPV TGNMGVVLPG EGFLQGVRRL TEEYGALLIF
DEVMTGFRIS YGGAQAHYGI DPDLTCLGKV IGGGLPVGAY GGKRRFMEQI SPSGPIYQAG
TLSGNPLAMN AGLTTLKLLQ QPGVYEELNR KTSRLAEGLK RIAKEAGLPV WVNALGAMFS
AFFTDVPVKD YASACTSDVE RFAKYFRGML EKGIYLAPSQ FEAVFLSAAH TDADIDNTLE
QARLVIKTL
//
