ID A0A1I6VJD0_9SPHI Unreviewed; 539 AA.
AC A0A1I6VJD0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05660206_11456 {ECO:0000313|EMBL:SFT13802.1};
OS Sphingobacterium wenxiniae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=683125 {ECO:0000313|EMBL:SFT13802.1, ECO:0000313|Proteomes:UP000198785};
RN [1] {ECO:0000313|EMBL:SFT13802.1, ECO:0000313|Proteomes:UP000198785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22789 {ECO:0000313|EMBL:SFT13802.1,
RC ECO:0000313|Proteomes:UP000198785};
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}.
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DR EMBL; FOZZ01000014; SFT13802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6VJD0; -.
DR STRING; 683125.SAMN05660206_11456; -.
DR Proteomes; UP000198785; 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; IPR022419; Porphobilin_deaminase_cofac_BS.
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.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 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:UP000198785};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00260}.
FT DOMAIN 15..225
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 328..521
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT MOD_RES 255
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ SEQUENCE 539 AA; 61045 MW; B1F39D746A081410 CRC64;
MRIFNRKLLK VNRKLIIGTR GSQLALWQAN FIKDRLAEIG VEAELKIIKT QGDIIQHLRL
DKLEGKGFFT KELEEELLSG QIDLAVHSHK DLPTVNPPGL IIACVSERED PSEVIIIHKD
CVDIKKRLSL KHNATVGTSS NRRKAQLLSL RPDLEFTDLR GNLQTRIQKL RDEKYDAIVL
AKAGVTRIEM DLSDFHLEEI PPIEVIPAPA QGVLAVQIRE SDRELFDLLQ PINDTEVAKT
IGVERKVLNM FDAGCHAPLG CYCRKTAEGK YEAWTSIAED NEDFPNRYYL QDDTTEGMAD
KIFAKYNKDR KLPSSVFITR DLDENSYLAR YLAKYNIQID ARSLIKIFPT INKLDSFILK
RADWIFFNSK NAIDHFFKLE PYILKKTKLA VLGRGSEDAL RKYDRVADFS GDNLGIKTED
IAKEFAKLVD GQTVFIPRAK DSLMSIQNAL TENTQVIDMP IYETVLEEEV DKTNAEVLIF
TSPSNVEAYF RENLVDPGQK IICIGHSTAK AIEAMGLPYT LPFTPDELGL AEAIFGLEI
//
