ID A0A094DAV4_9PEZI Unreviewed; 1236 AA.
AC A0A094DAV4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=V497_02031 {ECO:0000313|EMBL:KFY63389.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY63389.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY63389.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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:KFY63389.1}.
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DR EMBL; JPJZ01000489; KFY63389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DAV4; -.
DR STRING; 1420910.A0A094DAV4; -.
DR HOGENOM; CLU_267179_0_0_1; -.
DR OrthoDB; 9643at2759; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; IPR019383; Golgin_A_7/ERF4.
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; PF10256; Erf4; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 177..532
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT DOMAIN 1074..1192
FT /note="Golgin subfamily A member 7/ERF4"
FT /evidence="ECO:0000259|Pfam:PF10256"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 133391 MW; 10D0A97EEAA15B5F CRC64;
MCPFLKKTSP ATLRSLSATS GPTRSYHASP GGGSMSNLQT IARRCPVMGS AMAVQTAKTG
NAAFGAIAAL KGIRGFSGKA STGKAKLHTS STHEARPMEG ILMGENLPQV QPAKPVREAA
AVPENLVKKD GKFDYDAFYT NELDKKHKDK SYRHFNNINR LAKEFPRAHT ANPEERVTVW
CSNDYLGMGR NSNVLKAMHE TLDVYGAGAG GTRNISGHNQ HAVALEKTLA TLHAKEAALA
FTSCYVANDA TMATLGSRLP GCVWLSDSLN HNSMIVGIQH SGAKKMVFKH NDLADLEAKL
ASLPLSTPKI IAFESVYSMC GSVAPISEIC DLADKYGAIT FLDEVHAVGM YGPHGAGVAE
HLDYEAHVNG SPRGTVMDRV DIITGTLGKA YGCVGGYIAG SASMVDAVRS LAAGFIFTTT
LPPATMAGAR AAIEYQMSTQ SDRRLQQLHT RAVKDELAAR SIPVMDNPSH IIPVLVGTAE
LAKRASDLLL EKHGIYVQSI NYPTVPVGQE RLRITPTPGH TKEYRDHLVG ALESVWAELG
IKRTTDWAAE GGFLGVGSDE APIEPLWTDK QLGVEAAKGS NGKNQVLEHD IHSSTELPFR
AQLLRQKNPE FCAELNATSL RRQYPSAPLS GLAKSADRQR STFENQRQPN TLTTTTTSTP
TPQPPRNRRL SLFPHSTPHP GLATASPPTS SHPGPPPRAP TGLTPSPLPT PAVDEPAPPP
ASWPISHSSP SPPEPTTTRT ANPRLPAPSS QPPYPTPPTA ARRRWSLRNA FAPALLPQLP
DPRTQRLRLE AQRATRLWNP SNSTPRTRRP TTTATATTTH RGRARAASGS SVVQPAIPLR
HPQLTKGEIE GEIQGAGDIE FIGGKDKGGA GDYPLLSLRE QRFSRNSSGR ASLQVEYSAA
SSGTQSNRVS LPRSVTSIDI RRSFSLVAED FTAGATVEHE DKGKGKDIEG GRYSTERRST
GYRKRGQSIA SLHPPVALSP TFKQDIAPPL THTTRNYTMA DLESGPPTQS QPQNPYHDTT
DNLASLTSTH TSIHGSERPI TPGADDAWGP AHPCFPHLNP YVPLDSVAYA NTRIIRIPRD
WMVAGDLAPT FSATYPELLG EAGLGEAEFR RCVESINARL IEAFDPFGVR NLVDAVMGLC
TGWFWDDAGL TYTKRCLAAV EKAIEGFNRE LEMGSSQARF ISLKKSAYMS LDVQIPTPQI
GFIESEMDDD EDRASYAGAE QPIGERAETR DGEEAR
//
