ID G2KQI4_MICAA Unreviewed; 409 AA.
AC G2KQI4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=5-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00013257};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
DE AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|ARBA:ARBA00031691};
DE AltName: Full=Delta-ALA synthase {ECO:0000256|ARBA:ARBA00031945};
DE AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00032773};
GN Name=hemA {ECO:0000313|EMBL:AEP09120.1};
GN OrderedLocusNames=MICA_786 {ECO:0000313|EMBL:AEP09120.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09120.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP09120.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09120.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; CP002382; AEP09120.1; -; Genomic_DNA.
DR RefSeq; WP_014102343.1; NC_016026.1.
DR AlphaFoldDB; G2KQI4; -.
DR STRING; 856793.MICA_786; -.
DR KEGG; mai:MICA_786; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000009286; Chromosome.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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:0000313|EMBL:AEP09120.1};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Transferase {ECO:0000313|EMBL:AEP09120.1}.
FT DOMAIN 50..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 409 AA; 44823 MW; 19D5BF41929F1501 CRC64;
MTGFDYTGFF ADRITELKTE GRYRTFATLS RIAGRFPQAM YHAPDGTSRE VTIWCSNDYL
GMGQHPVVLN AMHEAIDACG SGAGGTRNIS GTTRYHVELE ATMARLHNKE AALVFTSGYT
ANEGALGTIG RMLPNCIIFS DALNHASMIH GMKSSGAEKA VFRHNDLAHL EELLQKADPK
RPKIVAFESV YSMEGDICPM AEIIALAEKY GALTYLDEVH GVGLYGPRGA GVAEERDLMD
RIDIIEGTFG KAYGLIGGYI AGRASIVDAV RSFASGFIFT TSLPPAVLAG AKASVEYLMN
SSIERQRQRA NVKRFKDRLT RDNLPFMQGE SHIVPLVVGD SSCCKLVTDI LLNDYNMYVQ
PINYPTVPKG TERMRLTATA AHSLDEVDAF ADILRDLWEE QHVAQYAAA
//
