HEM3_PROMS
ID HEM3_PROMS Reviewed; 316 AA.
AC A2BPX7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=A9601_05521;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {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; CP000551; ABM69838.1; -; Genomic_DNA.
DR RefSeq; WP_011818004.1; NC_008816.1.
DR AlphaFoldDB; A2BPX7; -.
DR SMR; A2BPX7; -.
DR STRING; 146891.A9601_05521; -.
DR EnsemblBacteria; ABM69838; ABM69838; A9601_05521.
DR KEGG; pmb:A9601_05521; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_0_2_3; -.
DR OMA; LWQANHI; -.
DR OrthoDB; 1450400at2; -.
DR UniPathway; UPA00251; UER00319.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000002590; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
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 Chlorophyll biosynthesis; Porphyrin biosynthesis; Transferase.
FT CHAIN 1..316
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000304258"
FT MOD_RES 245
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ SEQUENCE 316 AA; 35034 MW; F8CC2C27C152C850 CRC64;
MTNFKLKIAS RRSKLAMVQT LWVKDQLEKN IPNLEVSIEA MATQGDKILD VALAKIGDKG
LFTKELEAQM LVGHADIAVH SLKDLPTNLP NGLKLGCITK REDPADALVV NKKNDCYKLE
NLPEGSIVGT SSLRRLAQLR NKYPHLVFKD IRGNVITRIE KLDAGEFDCI ILAAAGLKRL
GFESRIHQII PSEVSLHAVG QGALGIECKS DDKKVLEIIS ILEDKPTCQR CLAERAFLRE
LEGGCQVPIG VNSKIQNEQL CLTGMVASLD GERLIKDQYI GDINDPEEVG KELAKKLKQQ
GAEEILSEIF KKFREK