ID G1LRB2_AILME Unreviewed; 701 AA.
AC G1LRB2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=5-aminolevulinate synthase, non-specific, mitochondrial {ECO:0000256|ARBA:ARBA00039790};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
DE AltName: Full=5-aminolevulinic acid synthase 1 {ECO:0000256|ARBA:ARBA00042303};
DE AltName: Full=Delta-ALA synthase 1 {ECO:0000256|ARBA:ARBA00042219};
DE AltName: Full=Delta-aminolevulinate synthase 1 {ECO:0000256|ARBA:ARBA00042079};
GN Name=ALAS1 {ECO:0000313|Ensembl:ENSAMEP00000009597.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000009597.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000009597.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000009597.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent
CC condensation of succinyl-CoA and glycine to form aminolevulinic acid
CC (ALA), with CoA and CO2 as by-products.
CC {ECO:0000256|ARBA:ARBA00037218}.
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:ARBA00033616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC Evidence={ECO:0000256|ARBA:ARBA00033616};
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: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004637}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR STRING; 9646.ENSAMEP00000009597; -.
DR Ensembl; ENSAMET00000010012.2; ENSAMEP00000009597.2; ENSAMEG00000009102.2.
DR Ensembl; ENSAMET00000038513.1; ENSAMEP00000031085.1; ENSAMEG00000009102.2.
DR Ensembl; ENSAMET00000047314.1; ENSAMEP00000042760.1; ENSAMEG00000009102.2.
DR eggNOG; KOG1360; Eukaryota.
DR GeneTree; ENSGT00940000156030; -.
DR HOGENOM; CLU_015846_6_1_1; -.
DR TreeFam; TF300724; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006784; P:heme A biosynthetic process; IEA:Ensembl.
DR GO; GO:0006785; P:heme B biosynthetic process; IEA:Ensembl.
DR GO; GO:0048034; P:heme O biosynthetic process; IEA:Ensembl.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903412; P:response to bile acid; IEA:Ensembl.
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:SF50; 5-AMINOLEVULINATE SYNTHASE, NON-SPECIFIC, MITOCHONDRIAL; 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 Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 63..199
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 307..651
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 77367 MW; 864D5EC90B715E6C CRC64;
MRSAPSGCIL GRQRSRPEAS RRQGQRVFSI WLGCLPPPSQ PPPPLPPPPQ CPAQDQCTLS
DMETVVRRCP FLSRVPQAFL QKAGKSLLFY AQNCPKMMEV GAKPAPRALS TSAVHCQQVK
ETPPANEKDK TAKAEVQQAA DGSQQTPDGT QLPSGHPSLA TSQGTASKCP FLAAQMSQKG
SNVFRKASLE LQEDVQEMHA VRKEVAQTSV NSSVISVKAD EGEPSGLLKN FQDIMRKQRP
ERVSHLLQDN LPKSVSTFQY DRFFEKKIDE KKNDHTYRVF KTVNRRAHIF PMADDYSDSL
ITKKQVSVWC SNDYLGMSRH PRVCGAVMET LKQHGAGAGG TRNISGTSKF HVDLEQELAD
LHGKDAALLF SSCFVANDST LFTLARMMPG CEIYSDSGNH ASMIQGIRNS RVPKYIFRHN
DVSHLRELLQ RSDPSVPKIV AFETVHSMDG AVCPLEELCD VAHEFGAITF VDEVHAVGLY
GARGGGIGDR DGVMPKMDII SGTLGKAFGC VGGYIASTSS LIDTVRSYAA GFIFTTSLPP
MLLAGALESV RILKSAEGRA LRRQHQRNVK LMRQMLMDAG LPVVHCPSHI IPVRVADAAK
NTEVCDELMS RHNIYVQAIN YPTVPRGEEL LRIAPTPHHT PQMMNYFLEN LLATWKRVGL
ELKPHSSAEC NFCRRPLHFE VMSEREKSYF SGMSKLVSAQ A
//
