ID   HEM3_DICDI              Reviewed;         325 AA.
AC   Q54P93;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Porphobilinogen deaminase;
DE            EC=2.5.1.61;
DE   AltName: Full=Heme biosynthesis protein C;
DE   AltName: Full=Hydroxymethylbilane synthase;
DE            Short=HMBS;
GN   Name=hemC; ORFNames=DDB_G0284697;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
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; AAFI02000070; EAL65118.1; -; Genomic_DNA.
DR   RefSeq; XP_638482.1; XM_633390.1.
DR   AlphaFoldDB; Q54P93; -.
DR   SMR; Q54P93; -.
DR   STRING; 44689.DDB0231417; -.
DR   PaxDb; Q54P93; -.
DR   PRIDE; Q54P93; -.
DR   EnsemblProtists; EAL65118; EAL65118; DDB_G0284697.
DR   GeneID; 8624733; -.
DR   KEGG; ddi:DDB_G0284697; -.
DR   dictyBase; DDB_G0284697; hemC.
DR   eggNOG; KOG2892; Eukaryota.
DR   HOGENOM; CLU_019704_0_2_1; -.
DR   InParanoid; Q54P93; -.
DR   OMA; LWQANHI; -.
DR   PhylomeDB; Q54P93; -.
DR   UniPathway; UPA00251; UER00319.
DR   PRO; PR:Q54P93; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; ISS:UniProtKB.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Heme biosynthesis; Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..325
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000327798"
FT   MOD_RES         253
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  36033 MW;  2498FEF3ACA97A1D CRC64;
     MSSITKRDKV IIGSRKSQLA MLQTEWVRDR IQELNPGIIV EIKTMDTTGD KVLDVSLSKI
     GDKGLFTKEL EDMMLNGTID LAVHSLKDIP TKLPDGLKLG AITKRYNTSD AFIANAKKHG
     KNCKLSELPQ GAMIGSSSLR RVAQLKKAYP HLQFKDIRGN LNTRFKKLED DSNGYDGMIL
     AVAGLERMEL TDHISEIIPD SISLYAVGQG SLGIECKDGD DFIQSILNPL IHRESMYCCE
     AERSMLRDLE GGCHVPIGVV TKLHNQSQPD ETLEINAIVL NLDGSKYIES KIIGPSIQYY
     QLGKSIAQDL INKGSKDILS EFIKK