ID A0A1W9H6H0_9PROT Unreviewed; 406 AA.
AC A0A1W9H6H0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=A4S12_05930 {ECO:0000313|EMBL:OQW43010.1};
OS Proteobacteria bacterium SG_bin5.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827382 {ECO:0000313|EMBL:OQW43010.1, ECO:0000313|Proteomes:UP000192868};
RN [1] {ECO:0000313|EMBL:OQW43010.1, ECO:0000313|Proteomes:UP000192868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin5 {ECO:0000313|EMBL:OQW43010.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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}.
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:OQW43010.1}.
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DR EMBL; LWDI01000045; OQW43010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9H6H0; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000192868; Unassembled WGS sequence.
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:SF102; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL; 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 Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 47..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 406 AA; 44099 MW; 73BD51D1E6D6C151 CRC64;
MDYDQFFADK LGELKADGRY RIFAELERRA GAFPRAAHYR EDGVGEVTVW CSNDYLGMGQ
HPAVTGAMHA TIDACGAGAG GTRNISGTCH AHVELERELA DLHAKEAALL FTSGYVSNWA
ALSTLASKLP NCVVLSDALN HASMIEGIRH SRAECRRFKH NDVADLDRLL SEVEPGRAKL
VAFESVYSMD GDIAPIEQII EVCEKHGALS YIDEVHAVGL YGPRGGGVAE ARGLMDRIDV
IEGTLGKAFG VMGGYITGSA ALVDFVRSFA SGFIFTTALP PALAAAATAS IRHLKVSQIE
RARHQERVAT VRRRLHAIGI PTLENPSHII PVMVGDAKKC KRISDWLLDH HGIYVQPINY
PTVPVGTERL RITPSPVHSD ADIDRLVTAL SEIWSMCELA RRAEAA
//