ID   HEM3_EUGGR              Reviewed;         480 AA.
AC   P13446;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Porphobilinogen deaminase, chloroplastic;
DE            Short=PBG;
DE            EC=2.5.1.61;
DE   AltName: Full=Hydroxymethylbilane synthase;
DE            Short=HMBS;
DE   AltName: Full=Pre-uroporphyrinogen synthase;
DE   Flags: Precursor;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2477247; DOI=10.1111/j.1432-1033.1989.tb15026.x;
RA   Sharif A.L., Smith A.G., Abell C.;
RT   "Isolation and characterisation of a cDNA clone for a chlorophyll synthesis
RT   enzyme from Euglena gracilis. The chloroplast enzyme hydroxymethylbilane
RT   synthase (porphobilinogen deaminase) is synthesised with a very long
RT   transit peptide in Euglena.";
RL   Eur. J. Biochem. 184:353-359(1989).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+);
CC         Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC       Note=Binds 1 dipyrromethane group covalently.;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; X15743; CAA33759.1; -; mRNA.
DR   PIR; S06109; IBEG.
DR   AlphaFoldDB; P13446; -.
DR   SMR; P13446; -.
DR   UniPathway; UPA00251; UER00319.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.160.40; -; 1.
DR   HAMAP; MF_00260; Porphobil_deam; 1.
DR   InterPro; IPR000860; HemC.
DR   InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
DR   InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR   InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR   PANTHER; PTHR11557; PTHR11557; 1.
DR   Pfam; PF01379; Porphobil_deam; 1.
DR   Pfam; PF03900; Porphobil_deamC; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF54782; SSF54782; 1.
DR   TIGRFAMs; TIGR00212; hemC; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing; Plastid;
KW   Porphyrin biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..139
FT                   /note="Chloroplast"
FT   CHAIN           140..480
FT                   /note="Porphobilinogen deaminase, chloroplastic"
FT                   /id="PRO_0000013324"
FT   MOD_RES         395
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  51744 MW;  269CE6CC195C0F3A CRC64;
     MYCGRYETIG ETRGNSLNVF IGAAAGFVAA VALINSGLAT SFYSTPVRAV PQVIVPSSLA
     ASSQLPVVPK ETNIQVNSAQ ILYPDSTVKG QERTITILGV CSFLSASLFY IWKQFGMKAR
     TTKPADLQEV SGGRIWSLAS TTGSNIGAGK TVRVATRKSP LAMWQAEFIQ SELERLWPGI
     TVELQPMSTR GDKILDSPLA KVGGKGLFVK ELETALLENR SDIAVHSTKD VPMELPEGLV
     LGVICKRHDP CDAIVFPKGS NLKSLEDLPH GARVGTSSLR RQCQLLLKRP DLKFLELRGN
     VNTRLAKLDS GDYDAIILAA AGLKRLGFSD RVLPGETNII DPNVMCPAAG QGALSIELRT
     NDPEIAALLE PLHHIPDAVT VACERAMNRR LNGGCQVPIS GFAQLKDGQL RMEARVGSVT
     GKGPLIIQSK TFRLPWSGRT WPQLQKESEA LGVEVADMLL ADGAQAYLDE AYASRTLGWA