HEM3_PSYIN
ID HEM3_PSYIN Reviewed; 310 AA.
AC A1T0R0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Ping_3642;
OS Psychromonas ingrahamii (strain 37).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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; CP000510; ABM05325.1; -; Genomic_DNA.
DR RefSeq; WP_011771873.1; NC_008709.1.
DR AlphaFoldDB; A1T0R0; -.
DR SMR; A1T0R0; -.
DR STRING; 357804.Ping_3642; -.
DR EnsemblBacteria; ABM05325; ABM05325; Ping_3642.
DR KEGG; pin:Ping_3642; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_0_2_6; -.
DR OMA; LWQANHI; -.
DR OrthoDB; 1450400at2; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000000639; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; 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 Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Porphobilinogen deaminase"
FT /id="PRO_1000047759"
FT MOD_RES 242
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ SEQUENCE 310 AA; 34210 MW; 9F593B4F1BDC1DEC CRC64;
MTAQKIRIAT RHSPLAMWQA NFIKSELLKY HPNLIVELLP MKTKGDIILD TPLAKVGGKG
LFVKELEVAI LEGRADIAVH SIKDVPVDFP EGLGLTTICK REDPHDAFVS NHYKQLDELP
EGAIVGTCSL RRQCQILALR PDIIIKNLRG NVNTRLRKLD EGEYDAIILA AAGLMRLEMQ
HRITSLIAPE VSLPAVGQGA VGIECRLDDE QTITLLKPLE DPETRIRITA ERAMNLKLQG
GCQVPIGSFA ILENEQLFLR GLVGSVDGKQ IIRKEITGHQ NDAQQLGITL AEQLLACGAE
EILAEVYKNQ