ID A0A367JXL1_RHIST Unreviewed; 554 AA.
AC A0A367JXL1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=5-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
DE EC=2.3.1.37 {ECO:0000256|RuleBase:RU910713};
DE AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|RuleBase:RU910713};
DE AltName: Full=Delta-ALA synthase {ECO:0000256|RuleBase:RU910713};
DE AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
GN Name=HEM1_1 {ECO:0000313|EMBL:RCH94670.1};
GN ORFNames=CU098_008543 {ECO:0000313|EMBL:RCH94670.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCH94670.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCH94670.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCH94670.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
CC -!- FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from
CC succinyl-CoA and glycine, the first and rate-limiting step in heme
CC biosynthesis. {ECO:0000256|ARBA:ARBA00003076}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU910713}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392,
CC 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:RCH94670.1}.
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DR EMBL; PJQM01002529; RCH94670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367JXL1; -.
DR STRING; 4846.A0A367JXL1; -.
DR EnsemblFungi; RCH94670; RCH94670; CU098_008543.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000253551; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IPR015118; 5aminolev_synth_preseq.
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 Pfam; PF09029; Preseq_ALAS; 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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|RuleBase:RU910713};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW Transferase {ECO:0000256|RuleBase:RU910713}.
FT DOMAIN 10..77
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 139..497
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 56..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 59973 MW; 92FB36BB68ED6A21 CRC64;
MEVALLQAKK SCPFIHVASA SSLRRLTSGP NINPLITKAK QCPVMSQAIS SRSISTSRAV
SQAPSKPAKA ATITGSHTRG PIDPTAVVSH QTKKHFDYES FYQEELEKKH KDKSYRYFNN
INRLAQKFPR AHTARVTDEV TVWCANDYLG MGRSPVLTDT MKRTLDRYGA GAGGTRNIAG
NADLHLRLES ELADLHHAEG ALVFSSCYVA NDATLSTLAS KLPGCVIFSD ALNHASMIQG
MRHSGAPKKI FRHNDMDHLE QLLQSVDPSV PKIIAFESVY SMCGSIGPIH KVVELAKKYG
AITFLDEVHA VGMYGSRGAG VAEHLDFELN AANPTRGNGS IMDEIDIYTG TLGKAYGVVG
GYIAGSASFV DMIRSYAPGF IFTTSLPPAV VSGALASVQY LKESNAERHL QQLNTRTVKS
RLGESGIPVI PNPSHIVPVL VGDAAAAKLA SDELLSEHNI YVQSINYPTV PVGEERLRIA
PCPGHSPEMI DHLVDSLETI WSRYGFKRVQ DWAAEGGCAS VGVPNAVEPT PIWTDKQLGL
DKIDEEQVVS NTVN
//
