ID C6S667_NEIML Unreviewed; 333 AA.
AC C6S667;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771, ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053, ECO:0000256|RuleBase:RU000515};
GN Name=hemB {ECO:0000313|EMBL:CBA05006.1};
GN OrderedLocusNames=NMO_0690 {ECO:0000313|EMBL:CBA05006.1};
OS Neisseria meningitidis (strain alpha14).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA05006.1, ECO:0000313|Proteomes:UP000002054};
RN [1] {ECO:0000313|EMBL:CBA05006.1, ECO:0000313|Proteomes:UP000002054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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 ECO:0000256|RuleBase:RU000515};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR EMBL; AM889136; CBA05006.1; -; Genomic_DNA.
DR RefSeq; WP_015815412.1; NC_013016.1.
DR AlphaFoldDB; C6S667; -.
DR KEGG; nmi:NMO_0690; -.
DR HOGENOM; CLU_035731_0_0_4; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000002054; Chromosome.
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 CDD; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
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.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515}.
FT ACT_SITE 202
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 257
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 333 AA; 36687 MW; 6D513AD02F7AA82E CRC64;
MQFPYRNVPA SRMRRMRRDD FSRRLMREHT LTADDLIYPV FVLEGSAREE DVPSMPGVKC
QSLDRLLFTA EEASNLGIPM LALFPVVTTN KTECAQEAYN PEGLVPTAVR ALRERFPELG
IMTDVALDPY TVHGQDGLTD ENGYVMNDET VEVLVKQALC HAEAGAQVVA PSDMMDGRIG
AIREALEDAG HIHARIMAYS AKYASAFYGP FRDAVGSSGN LGKADKKTYQ MDPANTDEAL
NEVALDIREG ADMVMVKPGL PYLDVVRRVK DEFGVPTYAY QVSGEYAMLQ AAIANGWLDG
GKVVLESLLA FKRAGADGIL TYYAIEAAKM LKR
//
