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Database: UniProt
Entry: A0A1M6W8D2_9BACT
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ID   A0A1M6W8D2_9BACT        Unreviewed;       324 AA.
AC   A0A1M6W8D2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Porphobilinogen deaminase {ECO:0000256|HAMAP-Rule:MF_00260};
DE            Short=PBG {ECO:0000256|HAMAP-Rule:MF_00260};
DE            EC=2.5.1.61 {ECO:0000256|HAMAP-Rule:MF_00260};
DE   AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|HAMAP-Rule:MF_00260};
DE            Short=HMBS {ECO:0000256|HAMAP-Rule:MF_00260};
DE   AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|HAMAP-Rule:MF_00260};
GN   Name=hemC {ECO:0000256|HAMAP-Rule:MF_00260};
GN   ORFNames=SAMN05720762_103346 {ECO:0000313|EMBL:SHK90024.1};
OS   Fibrobacter sp. UWH4.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896210 {ECO:0000313|EMBL:SHK90024.1, ECO:0000313|Proteomes:UP000184331};
RN   [1] {ECO:0000313|EMBL:SHK90024.1, ECO:0000313|Proteomes:UP000184331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWH4 {ECO:0000313|EMBL:SHK90024.1,
RC   ECO:0000313|Proteomes:UP000184331};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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:0000256|ARBA:ARBA00002869, ECO:0000256|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:0000256|ARBA:ARBA00000416, ECO:0000256|HAMAP-
CC         Rule:MF_00260};
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00260};
CC       Note=Binds 1 dipyrromethane group covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00260};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC   -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC       dipyrromethane group. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC   -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000256|ARBA:ARBA00005638,
CC       ECO:0000256|HAMAP-Rule:MF_00260}.
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DR   EMBL; FRAY01000003; SHK90024.1; -; Genomic_DNA.
DR   RefSeq; WP_072978459.1; NZ_FRAY01000003.1.
DR   AlphaFoldDB; A0A1M6W8D2; -.
DR   STRING; 1896210.SAMN05720762_103346; -.
DR   OrthoDB; 9810298at2; -.
DR   Proteomes; UP000184331; Unassembled WGS sequence.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 1.
DR   HAMAP; MF_00260; Porphobil_deam; 1.
DR   InterPro; IPR000860; HemC.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
DR   InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR   NCBIfam; TIGR00212; hemC; 1.
DR   PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR   PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 1.
DR   Pfam; PF01379; Porphobil_deam; 1.
DR   PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00260};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          6..209
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   MOD_RES         252
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   324 AA;  35100 MW;  B181BAD9927EDDE1 CRC64;
     MSEFKLRVAT RKSALAMAQT TMVAEAIVQA NPGLSYELVS MTTEGDRRLD KSLASFGGKG
     VFIKELEVAL LEGRADIAVH SLKDMPAEVL PEFKLAAVLH REDPRDAFVA RGGVDGCRFM
     ELPAGARIGT GSIRRVVQLK ALRPDLEYVP IRGNIQTRLS KLAELDGVVL AAAGLKRMGL
     ADQVTEFFST EHMLPASGQG ILAIETLSQL RHCEGNSPKQ SIDAILAHVN DAESYAIAVA
     EMAYLKALDA GCQFPVASFA EFVDTAATAD GVRELKIRGI YWDEISKRLL RAEILHSVSL
     ESPDLIAQSR AVGVALAQKI REQM
//
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