ID B9KI65_ANAMF Unreviewed; 346 AA.
AC B9KI65;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 Name=hemB {ECO:0000313|EMBL:ACM49177.1};
GN OrderedLocusNames=AMF_306 {ECO:0000313|EMBL:ACM49177.1};
OS Anaplasma marginale (strain Florida).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483 {ECO:0000313|EMBL:ACM49177.1, ECO:0000313|Proteomes:UP000007307};
RN [1] {ECO:0000313|EMBL:ACM49177.1, ECO:0000313|Proteomes:UP000007307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida {ECO:0000313|EMBL:ACM49177.1,
RC ECO:0000313|Proteomes:UP000007307};
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(2009).
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}.
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DR EMBL; CP001079; ACM49177.1; -; Genomic_DNA.
DR AlphaFoldDB; B9KI65; -.
DR STRING; 320483.AMF_306; -.
DR KEGG; amf:AMF_306; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_5; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000007307; 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 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, ECO:0000313|EMBL:ACM49177.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000007307}.
FT ACT_SITE 214
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 269
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 346 AA; 37927 MW; D067E54EB8A0158A CRC64;
MLHTVKENKL CVEERTEFQM QFPKTRMRRR RAHAWMRNIV RETALCAGNL ILPIFVHEHD
EDIIPVEGLD CMRNVSAKGA AHLAREALEA GINAVIVFPS RCKKSTDAEE AYNPNNLICG
AIRHIKDCVP EIGVIADVAL DPYTTSGHDG IVVDGEVDND ATITALCKQA AVLAAAGCDV
VAPSDMMDGR IGAIREFLDN CAFSNVCILS YAAKFCSCLY KPFRGVVGSR TMSQSIDKST
YQMDVANSRE ALLEARLDVD EGADMLMIKP GMFHLDVIAA VSAAVEVPVF AYQVSGEYAM
IKAASASGWL DYNQCMYEAL ISMKRAGARC IITYAALEVA RMLKTR
//
