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Database: UniProt
Entry: A0A0P1FTX5_THAGE
LinkDB: A0A0P1FTX5_THAGE
Original site: A0A0P1FTX5_THAGE 
ID   A0A0P1FTX5_THAGE        Unreviewed;       335 AA.
AC   A0A0P1FTX5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:CUH62777.1};
GN   ORFNames=TG4357_00295 {ECO:0000313|EMBL:CUH62777.1};
OS   Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH62777.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH62777.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH62777.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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}.
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DR   EMBL; CYSA01000003; CUH62777.1; -; Genomic_DNA.
DR   RefSeq; WP_058261088.1; NZ_FOFW01000003.1.
DR   AlphaFoldDB; A0A0P1FTX5; -.
DR   STRING; 53501.SAMN04488043_103195; -.
DR   OrthoDB; 9805001at2; -.
DR   UniPathway; UPA00251; UER00318.
DR   Proteomes; UP000051587; 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:UP000051587}.
FT   ACT_SITE        203
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"
SQ   SEQUENCE   335 AA;  36505 MW;  ECA331BCA5639B62 CRC64;
     MSHLGQAPFP KTRFRRTRQS PQIRALVQEN TLGVGDLIWP VFVRDGEGVE EPVASMPGVM
     RRSVDKIVEA AREAADLGIP VICLFPYTDP ALKTSTCEEA WNPDNLSNRA SRAIKDAGID
     IAVMSDVALD PYSADGHDGF VVDGKIINDE TVDALVKQAL SQARAGIDII GPSDMMDGRI
     GAMRDMLESE GFQDTMLLSY SAKYASAFYG PFRDAVGASG ALKGDKTTYQ MNPGNTDEAL
     RLIERDLSEG ADMVMVKPGM PYLDICRRVK DRFAVPTYAY QVSGEYAMIQ AAALNGWIDG
     EKAMMESLLC FKRAGCDGIL TYFAPAVAKK LHGLR
//
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