ID C4YW03_9RICK Unreviewed; 414 AA.
AC C4YW03;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=5-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00017999, 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 Name=hemA {ECO:0000313|EMBL:EER22423.1};
GN ORFNames=REIS_1646 {ECO:0000313|EMBL:EER22423.1};
OS Rickettsia endosymbiont of Ixodes scapularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=444612 {ECO:0000313|EMBL:EER22423.1, ECO:0000313|Proteomes:UP000007035};
RN [1] {ECO:0000313|Proteomes:UP000007035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=endosymbiont of Ixodes scapularis
RC {ECO:0000313|Proteomes:UP000007035};
RA Joardar V., Hostetler J., Durkin A.S., Gillespie J.J., Williams K.P.,
RA Daugherty S., Sakamoto J., Shukla M., Ferriera S., Shetty J., Schobel S.,
RA Steiner S.C., Sobral B.W.S., Hill C.A., Nene V., Caler E.;
RL Submitted (MAR-2009) 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}.
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DR EMBL; CM000770; EER22423.1; -; Genomic_DNA.
DR RefSeq; WP_008580668.1; NZ_CM000770.1.
DR AlphaFoldDB; C4YW03; -.
DR HOGENOM; CLU_015846_11_1_5; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000007035; 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 43..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 414 AA; 46333 MW; 02C59737A4AD2BDD CRC64;
MFYYNTIFSK HIDKIKSEGR YREFKALKRQ ADNFPFAEHA NKQIVMWCIN DYLGMSKHAK
VMQASIDALL KYGVGSGGTR NIGGNNIAIL ELEKELANLH KKQAALVFTS GFVANDTTLA
SLAKIMPDIV FFSDELNHAS IIAGITSSRA EKYIYRHLDV KHLEELLQSF DINRPKIIVF
ESAYSMDGFF SPIKDIINLA KKYNALTFID EVHTVGLYGK QGGGIAELLN CSDQIDIIQG
TLAKAYGTIG GYITSNHNLV DAIRLTAPGF IFTTSLPPVI STAATHSIRH LKESNEERIK
HQEVVTKLKN SFEHFNIPYL KNESHIVPII IGDPIKAAKT SNMLLNEYGI YVQHINFPTV
PRGTERLRII PTPAHTDKMI NDLSIALVQI FAELDIELSS AKELNEEVRL NLIA
//
