ID A0A1A0HGI4_9ASCO Unreviewed; 342 AA.
AC A0A1A0HGI4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=porphobilinogen synthase {ECO:0000256|ARBA:ARBA00012053};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN ORFNames=METBIDRAFT_34629 {ECO:0000313|EMBL:OBA23279.1};
OS Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA23279.1, ECO:0000313|Proteomes:UP000092555};
RN [1] {ECO:0000313|EMBL:OBA23279.1, ECO:0000313|Proteomes:UP000092555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA23279.1,
RC ECO:0000313|Proteomes:UP000092555};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC Binds two molecules of 5-aminolevulinate per subunit, each at a
CC distinct site, and catalyzes their condensation to form
CC porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00001227};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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:OBA23279.1}.
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DR EMBL; LXTC01000001; OBA23279.1; -; Genomic_DNA.
DR RefSeq; XP_018713760.1; XM_018856502.1.
DR AlphaFoldDB; A0A1A0HGI4; -.
DR STRING; 869754.A0A1A0HGI4; -.
DR GeneID; 30029478; -.
DR OrthoDB; 2782182at2759; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000092555; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR Pfam; PF00490; ALAD; 1.
DR PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 212
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 265
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 222
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 234
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 292
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 331
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 342 AA; 37868 MW; 9FD849EBA4945AD0 CRC64;
MSLHKAQYLS ESTTEISSIL QGGYNHPLAR EWQSERQLTK SMFIFPLFVS DIPDEETVME
SLPNIKRVGI KRLLQYVAPL VEKGLRAVIL FGVILKPGVK DEEGTPADDP EGPVISAIRL
LREKFPLLYI MCDVCLCEYT SHGHCGILHE DGTLKREKSV LRIGAVAVSY ARAGANCLAP
SDMMDGRIRE IKRGLIEAQL ENKVLVMSYS AKFSGSLYGP FRDIAGSVPS HGDRKLYQLP
SGGAGLARRA LLRDIEEGAD AFIVKPSTFY LDVVNEASKI CKDFPLCVYQ VSGEYAMLHA
AAEKGVVDLK AIAFESHHGF LRAGARLIIS YFTPEFLDWL DL
//
