HEM3_AQUAE
ID HEM3_AQUAE Reviewed; 304 AA.
AC O66621;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Porphobilinogen deaminase;
DE Short=PBG;
DE EC=2.5.1.61;
DE AltName: Full=Hydroxymethylbilane synthase;
DE Short=HMBS;
DE AltName: Full=Pre-uroporphyrinogen synthase;
GN Name=hemC; OrderedLocusNames=aq_263;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC06580.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000657; AAC06580.1; ALT_INIT; Genomic_DNA.
DR PIR; A70324; A70324.
DR RefSeq; NP_213181.1; NC_000918.1.
DR AlphaFoldDB; O66621; -.
DR SMR; O66621; -.
DR STRING; 224324.aq_263; -.
DR PRIDE; O66621; -.
DR EnsemblBacteria; AAC06580; AAC06580; aq_263.
DR KEGG; aae:aq_263; -.
DR PATRIC; fig|224324.8.peg.219; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_0_2_0; -.
DR InParanoid; O66621; -.
DR OMA; LWQANHI; -.
DR OrthoDB; 1450400at2; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000000798; Chromosome.
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 3: Inferred from homology;
KW Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000142902"
FT MOD_RES 236
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 304 AA; 34031 MW; FE9C210FA81DEE6B CRC64;
MKIRIGTRKS KLALWQANYV KDFLEKHWGV EVELVKITTT GDKITDVPLA KIGGKGLFVK
EIEKALLEGS IDLAVHSLKD VPMVIPKGLK LGAITKRENP YDVLISRSGK KLYELPSGSV
IGTSSLRRQV QIKKRRRDLK VEVLRGNVDT RMRKLKEGLY DAVILAYAGV KRMGYESEIT
EVLEDFIPAV GQGSLAIEIR EGDKRIEELI KPLNNEESFL CAIAERTFLR RLEGGCQVPV
GAFAKIENGT LKMKAFISDI EAERYIEGYR EGNPEEAEKL GLSLAEELLK KGGEEILKEI
YSSQ