ID Q8YGG2_BRUME Unreviewed; 345 AA.
AC Q8YGG2; D0B2I3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 OrderedLocusNames=BMEI1197 {ECO:0000313|EMBL:AAL52378.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL52378.1, ECO:0000313|Proteomes:UP000000419};
RN [1] {ECO:0000313|EMBL:AAL52378.1, ECO:0000313|Proteomes:UP000000419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094
RC {ECO:0000313|Proteomes:UP000000419};
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA Haselkorn R., Kyrpides N., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52378.1; -; Genomic_DNA.
DR PIR; AG3401; AG3401.
DR RefSeq; WP_002963896.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YGG2; -.
DR GeneID; 55590474; -.
DR KEGG; bme:BMEI1197; -.
DR KEGG; bmel:DK63_213; -.
DR PATRIC; fig|224914.52.peg.220; -.
DR eggNOG; COG0113; Bacteria.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000000419; Chromosome I.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515}.
SQ SEQUENCE 345 AA; 38069 MW; 2503C992BEF9E097 CRC64;
MTDRQSKYLP ANISQHVDDV TGSRRLRRMR KADWSRRLVQ ENHLTVNDLI LSFFLTYGSG
VTEPVEAMPG VERYSVDMAV RMAEKAARLG IPAIAPFPRE KPEVKTDDGS FVANPDNLIN
RAVRAIKKEV PEIGIITDAA LDPFTTHGHD GILRDGEILN DESVAMVVRG ALSQAEAGAD
IIAPSDMMDG RVGAVRQALD EHGFSHVPIM SYATKFASAF YGPYRGAIGT QGLLKGDKKT
YYIDPANPEE AVREAEQDIA EGADMLMVKP GLPYLDIIHR LKDEFRLPTF AYQVSGEYAM
IKAAGINGWI DEEKVMMESL LAFKRAGCDG ILTYFAMEVA EKLKA
//