ID A0A0C9LQ03_9FUNG Unreviewed; 859 AA.
AC A0A0C9LQ03;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=5-aminolevulinate synthase, mitochondrial {ECO:0000256|ARBA:ARBA00019560};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
DE AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|ARBA:ARBA00031691};
DE AltName: Full=Delta-ALA synthase {ECO:0000256|ARBA:ARBA00031945};
DE AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|ARBA:ARBA00032773};
GN ORFNames=MAM1_0005c00576 {ECO:0000313|EMBL:GAN01145.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN01145.1};
RN [1] {ECO:0000313|EMBL:GAN01145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN01145.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005029}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR EMBL; DF836294; GAN01145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LQ03; -.
DR STRING; 91626.A0A0C9LQ03; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
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 InterPro; IPR005606; Sec20.
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; PF03908; Sec20; 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 Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 216..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 444..802
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 361..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94147 MW; BCBE350D5D3C7D9E CRC64;
MTSIENSFRS LSRLAAECQR QVERLYHVDS ITVQKEVAEL IRSSIRCLAT DIEVVKQLAE
EQDTESSKMN ILNRLGEYEN QLRQLQVSSR QAILRSKKRV DEEEKRNREE LFGIGPKRLN
GKSFTEQYEL KQKGLQRGQH DEAVLRASSD VTEALKRTST LMQQELEKST FSASMLAESS
KTLTSTYTEY QNLGSLIHIS KRVITQLEAS DWFDRLLLLF GVLLFSSVVL YIIKKRTWDV
GISWVSWLSQ TKKSKETLAT TIVTVIAQST LSAIATTTSS TTPTATTTLL DSLIETASPA
IAGIIALMQA KKSCPFIHVA SASSLRRLTT GSSANQAMSP LMTKAKQCPI MSKAIQSRSI
STSNVASQSP SKPVKATAVT NHGQGPIPAA TAVSHQTKKH FDYESFYQEE LDKKHKDKSY
RYFNNINRLA QKFPRAHTAR VTDEVTVWCA NDYLGMGRSP VLTDTMKHTL DRYGAGAGGT
RNIAGNADLH LRLESELADL HHTEGALVFS SCYVANDATL STLASKLPGC VIFSDALNHA
SMIQGMRHSG APKKIFRHND MEHLEQLLQS VDPSVPKIIA FESVYSMCGS IGPIRQIVDL
AKKYGAITFL DEVHAVGMYG PRGAGVAEHL DYDLNAANPT MGNGSILDEI DIVTGTLGKA
YGVVGGYIAG SAYLVDMIRS YAPGFIFTTS LPPAVVSGAM ESVKYLKESS AERSLQQINT
RTVKSRLGNI GIPVIPNPSH IVPVLVGDAA AAKLASDELL SEHDIYVQSI NYPTVPVGEE
RLRITPTPGH NAPMIDELVH SLDKIWTRYG FKRLEDWSAQ GGCAGVGVEN AVEPTPMWTD
KQLGLDKVVD SQQAASNTN
//
