ID   HEM3_BOVIN              Reviewed;         361 AA.
AC   Q2KIN5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Porphobilinogen deaminase {ECO:0000305};
DE            EC=2.5.1.61 {ECO:0000250|UniProtKB:P08397};
DE   AltName: Full=Hydroxymethylbilane synthase;
DE            Short=HMBS;
GN   Name=HMBS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As part of the heme biosynthetic pathway, catalyzes the
CC       sequential polymerization of four molecules of porphobilinogen to form
CC       hydroxymethylbilane, also known as preuroporphyrinogen. Catalysis
CC       begins with the assembly of the dipyrromethane cofactor by the
CC       apoenzyme from two molecules of porphobilinogen or from
CC       preuroporphyrinogen. The covalently linked cofactor acts as a primer,
CC       around which the tetrapyrrole product is assembled. In the last step of
CC       catalysis, the product, preuroporphyrinogen, is released, leaving the
CC       cofactor bound to the holodeaminase intact.
CC       {ECO:0000250|UniProtKB:P08397}.
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:0000250|UniProtKB:P08397};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13186;
CC         Evidence={ECO:0000250|UniProtKB:P08397};
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC         Evidence={ECO:0000250|UniProtKB:P08397};
CC       Note=Binds 1 dipyrromethane group covalently.
CC       {ECO:0000250|UniProtKB:P08397};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000250|UniProtKB:P08397}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08397}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR   EMBL; BC112573; AAI12574.1; -; mRNA.
DR   RefSeq; NP_001039672.1; NM_001046207.1.
DR   AlphaFoldDB; Q2KIN5; -.
DR   SMR; Q2KIN5; -.
DR   STRING; 9913.ENSBTAP00000007052; -.
DR   PaxDb; Q2KIN5; -.
DR   PRIDE; Q2KIN5; -.
DR   Ensembl; ENSBTAT00000007052; ENSBTAP00000007052; ENSBTAG00000005364.
DR   GeneID; 515614; -.
DR   KEGG; bta:515614; -.
DR   CTD; 3145; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005364; -.
DR   VGNC; VGNC:29870; HMBS.
DR   eggNOG; KOG2892; Eukaryota.
DR   GeneTree; ENSGT00390000009083; -.
DR   HOGENOM; CLU_019704_0_1_1; -.
DR   InParanoid; Q2KIN5; -.
DR   OMA; LWQANHI; -.
DR   OrthoDB; 1189095at2759; -.
DR   TreeFam; TF105389; -.
DR   Reactome; R-BTA-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000005364; Expressed in longissimus thoracis muscle and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Heme biosynthesis; Phosphoprotein; Porphyrin biosynthesis;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P08397"
FT   CHAIN           2..361
FT                   /note="Porphobilinogen deaminase"
FT                   /id="PRO_0000244405"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08397"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08397"
FT   MOD_RES         74
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22907"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08397"
FT   MOD_RES         261
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39515 MW;  15596E68C92E80C9 CRC64;
     MSGNGNAAAI AEEDTPKMRV IRVGTRKSQL ARIQTDSVVA TLKALYPGLQ FEIIAMSTTG
     DKILDTALSK IGEKSLFTKE LEHALERNEV DLVVHSLKDL PTVLPPGFTI GAVCKRESPY
     DAVVFHPKFV GKTLETLPEK SVVGTSSLRR AAQLQRKFPH LEFKSIRGNL NTRLRKLDEL
     QEFSAIILAT AGLQRMGWQN RVGQILHPEE CMYAVGQGAL GVEVRAKDQD ILDLVGVLHD
     PETLLRCIAE RSFLRHLEGG CSVPVAVHTA IKDGQLYLTG GVWSLNGAET MQDTMQTTIH
     VPVQHEDGPE DDPQLVGITA RNIPRQPQLA AENLGISLAT LLLNKGAKNI LDVARQLNEA
     H