ID A0A1G7MEL8_9SPHI Unreviewed; 552 AA.
AC A0A1G7MEL8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05216464_12136 {ECO:0000313|EMBL:SDF59640.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDF59640.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDF59640.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDF59640.1,
RC ECO:0000313|Proteomes:UP000199072};
RA de Groot N.N.;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNAI01000021; SDF59640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7MEL8; -.
DR STRING; 1391627.SAMN05216464_12136; -.
DR Proteomes; UP000199072; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06578; HemD; 1.
DR Gene3D; 3.40.50.10090; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_00260; Porphobil_deam; 1.
DR InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
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; PF02602; HEM4; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF69618; HemD-like; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000199072};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00260}.
FT DOMAIN 33..243
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 350..541
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT MOD_RES 273
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ SEQUENCE 552 AA; 61445 MW; 785FDAF6EABC4DC0 CRC64;
MQLEKIAEID VPYHQHKKLN LQLKTSILLD RKLIIGTRGS ELALWQANFI KDSLAAINIT
AELKIIKTQG DRILNLSFDK LEGKGFFTKE LEEELLAGTI DLAVHSHKDL PTENPPGLII
AAVSEREDPA ELLLILKDCV DVHQKLSVKY GAIVGTSSNR RKAQLLAYRP DLEITDLRGN
VPTRIGKLRD EKYDAIMLAK AGVSRLGIDL SEFHVEELTP AELIPAPAQG ALAIQIREVD
QELFESLQAL HHADVAEELA VERTVLKLFG GGCHLPLGCY CRRDEGMFQV FTSKANEGDE
FPDRLFIEAA TTEGLAERVV AKFSKDRKFP GKVFISRELS DQSYFKKSME NRNIQIEARS
LIRTVPVITK LDSYILRNID WVFFSSKNAV EYFFQLNPQF PKKVKFGVMG SGSEEMLRRK
GYFTDYVGEG TDTAEVAEEF AKLANGTIVL FPGAEGSMRS IQQGLSADTK IIDLPVYETV
LEEEVEASGA DVLVFTSPSN VEAYFADNLL DPYQKVVAIG KSTGKKFDEM GVKYTLPYSP
DEVGLAEAVF GL
//
