HEM3_CLOB6
ID HEM3_CLOB6 Reviewed; 290 AA.
AC C3L2Z3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Porphobilinogen deaminase {ECO:0000255|HAMAP-Rule:MF_00260};
DE Short=PBG {ECO:0000255|HAMAP-Rule:MF_00260};
DE EC=2.5.1.61 {ECO:0000255|HAMAP-Rule:MF_00260};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000255|HAMAP-Rule:MF_00260};
DE Short=HMBS {ECO:0000255|HAMAP-Rule:MF_00260};
DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000255|HAMAP-Rule:MF_00260};
GN Name=hemC {ECO:0000255|HAMAP-Rule:MF_00260}; OrderedLocusNames=CLJ_B0971;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC {ECO:0000255|HAMAP-Rule:MF_00260}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00260};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00260};
CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000255|HAMAP-
CC Rule:MF_00260};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000255|HAMAP-
CC Rule:MF_00260}.
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DR EMBL; CP001083; ACQ54939.1; -; Genomic_DNA.
DR RefSeq; WP_003360878.1; NC_012658.1.
DR AlphaFoldDB; C3L2Z3; -.
DR SMR; C3L2Z3; -.
DR EnsemblBacteria; ACQ54939; ACQ54939; CLJ_B0971.
DR KEGG; cbi:CLJ_B0971; -.
DR HOGENOM; CLU_019704_0_2_9; -.
DR OMA; LWQANHI; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000002333; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis; Transferase.
FT CHAIN 1..290
FT /note="Porphobilinogen deaminase"
FT /id="PRO_1000204647"
FT MOD_RES 237
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ SEQUENCE 290 AA; 32827 MW; 7C38AB02333809A6 CRC64;
MNFIIATRRS KLAQVQTEII IDLLNKKHDI ECEKLLIETV GDKILEVSLD KIGGKGLFVK
DIEVAMLEQR ADAAVHSMKD VPYEMPKGFE IIAIPEREDV RDAFISLDNI KFKDLREGAK
IGTSSRRRAA QLKLLRSDLD IVPIRGNVQT RIEKIKKENL DGIILAVAGL KRVNLDHLIT
DYFDTKEMVP AIGQGALGIE VMEEHPKKEL FKDLDHYNSK ICVLAERAFM RELDGDCHST
IGAYASIKDN IMHIIGIFER KNKIIKKEIT GTKDQYEKLG IALAEHILKD