ID W8S060_9RHOB Unreviewed; 404 AA.
AC W8S060;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=roselon_01110 {ECO:0000313|EMBL:AHM03507.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM03507.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM03507.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004372; AHM03507.1; -; Genomic_DNA.
DR RefSeq; WP_025311374.1; NZ_CP004372.1.
DR AlphaFoldDB; W8S060; -.
DR STRING; 1294273.roselon_01110; -.
DR KEGG; red:roselon_01110; -.
DR PATRIC; fig|1294273.3.peg.1088; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000019593; 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 Reference proteome {ECO:0000313|Proteomes:UP000019593};
KW Transferase {ECO:0000256|RuleBase:RU910713, ECO:0000313|EMBL:AHM03507.1}.
FT DOMAIN 46..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 44526 MW; AD013D566AA34B16 CRC64;
MSFDVLFQAQ LDELKEEGNY RIFAELERQC GTFPKVVNHH DDGKRDVTVW CSNDYLGMGQ
NPKVVQAMVD AVRSCGTGAG GTRNISGNAW HHKRLEEELA DLHNKEAALL FTSGYVSNWA
ALSTLGARLP NAVILSDELN HASMIEGIRH SRAQKVIWKH NDPEDLDRKL ATLPANATKI
VAFESVYSMD GDIAPIAEIL DVCEKHGAMS YIDEVHAVGM YGPRGGGVAE REGLMDRITL
IEGTLGKAYG CVGGYITGSH ALVDFVRSFA SGFIFTTALP PAVAAAATTS IRHLKESSYE
RDMQKRQVAR LRARLDAEGI PHVNNPSHII PVMVKDPVKC RMLSDILMDQ FGIYVQPINY
PTVPKGTERL RFTPGPLHTD DDIEYLVMAL KTLWKQCAIS HAVA
//
