ID Q98B77_RHILO Unreviewed; 425 AA.
AC Q98B77;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=5-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00013257, ECO:0000256|RuleBase:RU910713};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257, ECO:0000256|RuleBase:RU910713};
DE AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|ARBA:ARBA00031691, ECO:0000256|RuleBase:RU910713};
DE AltName: Full=Delta-ALA synthase {ECO:0000256|ARBA:ARBA00031945, ECO:0000256|RuleBase:RU910713};
DE AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00032773, ECO:0000256|RuleBase:RU910713};
GN OrderedLocusNames=mll5695 {ECO:0000313|EMBL:BAB52095.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB52095.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB52095.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:356416; EC=2.3.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00001588,
CC ECO:0000256|RuleBase:RU910713};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005029, ECO:0000256|RuleBase:RU910713}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; BA000012; BAB52095.1; -; Genomic_DNA.
DR RefSeq; WP_010913433.1; NC_002678.2.
DR AlphaFoldDB; Q98B77; -.
DR KEGG; mlo:mll5695; -.
DR PATRIC; fig|266835.9.peg.4528; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06454; KBL_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 InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01821; 5aminolev_synth; 1.
DR PANTHER; PTHR13693:SF105; 5-AMINOLEVULINATE SYNTHASE; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU910713};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW ECO:0000256|RuleBase:RU910713};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 46..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 425 AA; 45960 MW; EE51701D8E50293D CRC64;
MNYQRFFEEA IDQLHAERRY RVFADLERIA GKFPRAIWRS NGRAEEITVW CSNDYLGMGQ
HPDVIAAFQN AAGKMGSGAG GTRNISGTSN PLVELEHELA DLHGKDAALV FTSGFVSNEA
SISTIARLLP NCLIISDELN HASMIEGVRR SGAEKKIFRH NDVAHLESLL QAAGRERAKL
IVFESVYSMD GDIAPIREIV ELAERYNAMT YIDEVHAVGM YGPRGGGITE REGLADRIDI
IEGTLAKAFG TLGGYITGTS AVIDAVRSYA PGFIFTTALP PAIAAAATTS IRHLKRSQAE
RDAQQQQAAR TKQILSAAGL PVMESPTHIV PVLVGDPELC KMASDRLLGV HGIYIQPINY
PTVPRGTERL RITPTPFHSD ALIAGLQDAL VETWDALGIP YGAAGRPAVA KSDRIVPLLV
PKSGG
//
