ID   A0A161HS39_9EUGL        Unreviewed;       517 AA.
AC   A0A161HS39;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   12-AUG-2020, entry version 12.
DE   RecName: Full=5-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00013257};
DE            EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
OS   Perkinsela sp. SMB-60.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC   Ichthyobodonidae; Perkinsela; unclassified Perkinsela.
OX   NCBI_TaxID=1840652 {ECO:0000313|EMBL:ANB27657.1};
RN   [1] {ECO:0000313|EMBL:ANB27657.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SMB-60 {ECO:0000313|EMBL:ANB27657.1};
RX   PubMed=27193376; DOI=10.1186/s12862-016-0664-6;
RA   Cenci U., Moog D., Curtis B.A., Tanifuji G., Eme L., Lukes J.,
RA   Archibald J.M.;
RT   "Heme pathway evolution in kinetoplastid protists.";
RL   BMC Evol. Biol. 16:109-109(2016).
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|ARBA:ARBA00008392,
CC       ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; KU609011; ANB27657.1; -; mRNA.
DR   UniPathway; UPA00251; UER00375.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003693};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          133..483
FT                   /note="Aminotran_1_2"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          29..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  56588 MW;  EFC376E929C39D48 CRC64;
     MSLPNNVMSR FAQPKRAALL NFTSQVMHKS TQKPKGKACK QIPKTSKRKP IGEQMASPPV
     QCPYHHLHTP ITPSVTVIPS RQPVASPSYD QFFENYVQQI KTEGRYRVFT EVSRQERRHP
     RITWHAPNGK EKPVTVWCSN DYVCMSQHPA VVRAARNSLS THGVGAGGTR NISGNSHSIA
     ALEKDIAQWH GKAQGLVFSS GYVANEAALS ALGSILPETV FISDEENHAS MIMGMMHARG
     ASRKIWKHNN VEHLRELLIQ TRLNHPNASV VIAFESVYSM SGTIAPVREI VDLAKQFNAL
     TYVDEVHAVG LYGHTGTGLC ESLGLAGSID IIMGTLGKAV GVFGGYIASS STIVDALRCR
     APGFIFTTAL PPMIADAARK SIAVLAGDEG RGHRARFNAA HNYMKKLFVE NGLPIHPGES
     HILPLLVLDS TLCKRASDLL LNTHGHYVQP INYPTVPQGR ERLRITPGAK HTKKMCDSLL
     EAVLSVWKAL GLPLHHSYVA ANPYGRCPVM LSSRKLP
//