ID A0A161HS39_9EUGL Unreviewed; 517 AA. AC A0A161HS39; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 25-MAY-2022, entry version 16. 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 -!- 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}. 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; KU609011; ANB27657.1; -; mRNA. DR UniPathway; UPA00251; UER00375. 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 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; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. 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 //