ID A0A0P8YA40_9RHOB Unreviewed; 332 AA.
AC A0A0P8YA40;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 03-MAY-2023, entry version 20.
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 ORFNames=JI58_07300 {ECO:0000313|EMBL:KPU83843.1};
OS Marinosulfonomonas sp. PRT-SC04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marinosulfonomonas.
OX NCBI_TaxID=1527300 {ECO:0000313|EMBL:KPU83843.1, ECO:0000313|Proteomes:UP000054415};
RN [1] {ECO:0000313|EMBL:KPU83843.1, ECO:0000313|Proteomes:UP000054415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRT-SC04 {ECO:0000313|EMBL:KPU83843.1};
RA Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT Rico Trench Inferred From Single Cell Genomes.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPU83843.1}.
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DR EMBL; JPUR01000224; KPU83843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8YA40; -.
DR PATRIC; fig|1527300.3.peg.1548; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000054415; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054415}.
FT ACT_SITE 202
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 256
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
SQ SEQUENCE 332 AA; 35683 MW; 989CF43941B6EE5E CRC64;
MQPIPASFPA SRLRRTRCSA PLRALCQENE LSVNGLIWPV FVIEGVGVRQ PVASMPGVDR
LSIDLLVEVA REARDLGIPA ICIFPYTDPA LKTDCCREAW SADNLSNRAI SAVKSAVPEV
AVMTDIALDP YNSHGHDGIV KEGLIVNDET VETLVKMAMA QADAGADILG PSDMMDGRIG
AIRNALETAG HKDVAILSYS AKYASAYYGP FRDAVGASSA LKGDKKTYQM NPANSDEALR
LVARDLSEGA DMVMIKPGLP YLDICQRVKA KFGVPTFAYQ VSGEYAMIQA AAQNGWIDGD
AVMMESMMAF RRAGCDGVLT YFAPRVARAL NG
//
