ID B6IMU1_RHOCS Unreviewed; 352 AA.
AC B6IMU1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ACI98757.1};
GN OrderedLocusNames=RC1_1353 {ECO:0000313|EMBL:ACI98757.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98757.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI98757.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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; CP000613; ACI98757.1; -; Genomic_DNA.
DR AlphaFoldDB; B6IMU1; -.
DR STRING; 414684.RC1_1353; -.
DR KEGG; rce:RC1_1353; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_5; -.
DR OrthoDB; 9805001at2; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000001591; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 274
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
SQ SEQUENCE 352 AA; 38669 MW; B4B4CA7A4C35A1AC CRC64;
MPHDPAHHDD HHSHPHEPAP PPVGAYPRIR MRRNRADAWT RRMVSENRLT ADDLIWPVFI
LPGENRREPV PSMPGVERLS IDLLVPAVAE AAELGIPCVA LFPANPPEVK DPMGRESANP
DNLMCRAMRA LKRQVPDIGL FGDVALDPYT SHGHDGILRD GRIVNDETVE VLVRQALVQA
DAGCDIVGPS DMMDGRIGAI REALDAHGHQ GVRICAYSAK YASAFYGPFR DAVNTGALLT
GDKKTYQMDP ANSDEALREV QLDLQEGADM VMVKPGLPYL DIIRRVKDTF RVPTLAYNVS
GEYAMLKAAA ANGWLNYDKA MLEMLLAFKR SGADAVLTYA AIEAAKLLRQ QG
//
