HEM3_PEA
ID HEM3_PEA Reviewed; 369 AA.
AC Q43082;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 101.
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;
GN Name=HEMC;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Little Marvel; TISSUE=Leaf;
RX PubMed=7516080; DOI=10.1104/pp.103.1.139;
RA Witty M., Wallace-Cook A.D.M., Albrecht H., Spano A.J., Michel H.,
RA Shabanowitz J., Hunt D.F., Timko M.P., Smith A.G.;
RT "Structure and expression of chloroplast-localized porphobilinogen
RT deaminase from pea (Pisum sativum L.) isolated by redundant polymerase
RT chain reaction.";
RL Plant Physiol. 103:139-147(1993).
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; X73418; CAA51820.1; -; mRNA.
DR PIR; S35873; JQ2278.
DR AlphaFoldDB; Q43082; -.
DR SMR; Q43082; -.
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 PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 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..46
FT /note="Chloroplast"
FT CHAIN 47..369
FT /note="Porphobilinogen deaminase, chloroplastic"
FT /id="PRO_0000013323"
FT MOD_RES 303
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 39931 MW; F7660D8390894431 CRC64;
MEMTLYSSSS FSLPSAPSNP SLSLFTSSFR FSSFKTSPFS KCRIRASLAV EQQTQQNKTA
LIRIGTRGSP LALAQAHETR DKLMASHTEL AEEGAIQIVI IKTTGDKILS QPLADIGGKG
LFTKEIDEAL INGDIDIAVH SMKDVPTYLP EETILPCNLP REDVRDAFIS LSAASLADLP
AGSVIGTASL RRKSQILHRY PSLTVQDNFR GNVQTRLRKL SEGVVKATLL ALAGLKRLNM
TENVTSTLSI DDMLPAVAQG AIGIACRSND DKMAEYLASL NHEETRLAIS CERAFLTTLD
GSCRTPIAGY ASRDKDGNCL FRGLVASPDG TRVLETSRIG SYTYEDMMKI GKDAGEELLS
RAGPGFFNS