ID Q2FTL1_METHJ Unreviewed; 321 AA. AC Q2FTL1; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 89. DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771}; DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053}; DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837}; GN OrderedLocusNames=Mhun_2561 {ECO:0000313|EMBL:ABD42260.1}; OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / OS JF-1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum. OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42260.1, ECO:0000313|Proteomes:UP000001941}; RN [1] {ECO:0000313|Proteomes:UP000001941} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1 RC {ECO:0000313|Proteomes:UP000001941}; RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8; RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H., RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M., RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.; RT "Complete genome sequence of Methanospirillum hungatei type strain JF1."; RL Stand. Genomic Sci. 11:2-2(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 5-aminolevulinate = porphobilinogen + 2 H2O + H(+); 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:ARBA00047651}; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000254; ABD42260.1; -; Genomic_DNA. DR AlphaFoldDB; Q2FTL1; -. DR FunCoup; Q2FTL1; 227. DR STRING; 323259.Mhun_2561; -. DR EnsemblBacteria; ABD42260; ABD42260; Mhun_2561. DR KEGG; mhu:Mhun_2561; -. DR eggNOG; arCOG04300; Archaea. DR HOGENOM; CLU_035731_0_0_2; -. DR InParanoid; Q2FTL1; -. DR UniPathway; UPA00251; UER00318. DR Proteomes; UP000001941; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter. DR GO; GO:0006783; P:heme biosynthetic process; IEA:TreeGrafter. DR CDD; cd00384; ALAD_PBGS; 1. DR FunFam; 3.20.20.70:FF:000019; Delta-aminolevulinic acid dehydratase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR001731; ALAD. DR InterPro; IPR013785; Aldolase_TIM. DR NCBIfam; NF006762; PRK09283.1; 1. 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, ECO:0000313|EMBL:ABD42260.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244}; KW Reference proteome {ECO:0000313|Proteomes:UP000001941}; KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}. FT ACT_SITE 191 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1" FT ACT_SITE 244 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3" FT BINDING 201 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 213 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 229 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5" FT BINDING 269 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" FT BINDING 308 FT /ligand="5-aminolevulinate" FT /ligand_id="ChEBI:CHEBI:356416" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2" SQ SEQUENCE 321 AA; 35167 MW; 03B1AA011DE76AE0 CRC64; MRRLRRQKII PLLAETHIGK DDLIAPLFFD ENIAEPVPIL AMPGQNRWPV SMAAEVVTRM RTAGIRAVLL FGIPSVKDAE ASGAYAPEGV IQQVIRAMKK TCPDMVIITD LCACEYTDHG HCGYVGECCD GPNLLNDASL EMMQRIAVSQ AEAGADIVAP SCMLDGMVAA IREALDDYGH QEVLIMSYSS KFASALYGPF REAAGSGFSF GDRTGYQAPV SNRREAYRES EQDAAEGADI LMVKPAGWFG DVITDIKQLG LPVAAYQVSG EYSMIRAATE MGWLDERRVV MESLVSLKRA GADLIITYFA EDVCRWLSEH E //