ID A0A1G6RLR3_9ACTN Unreviewed; 342 AA.
AC A0A1G6RLR3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=SAMN04489747_0045 {ECO:0000313|EMBL:SDD04856.1};
OS Auraticoccus monumenti.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Auraticoccus.
OX NCBI_TaxID=675864 {ECO:0000313|EMBL:SDD04856.1, ECO:0000313|Proteomes:UP000198546};
RN [1] {ECO:0000313|EMBL:SDD04856.1, ECO:0000313|Proteomes:UP000198546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MON 2.2 {ECO:0000313|EMBL:SDD04856.1,
RC ECO:0000313|Proteomes:UP000198546};
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}.
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};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|ARBA:ARBA00001916};
CC -!- SIMILARITY: Belongs to the HMBS family.
CC {ECO:0000256|ARBA:ARBA00005638}.
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DR EMBL; LT629688; SDD04856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6RLR3; -.
DR STRING; 675864.SAMN04489747_0045; -.
DR Proteomes; UP000198546; Chromosome i.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
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 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 NCBIfam; TIGR00212; hemC; 1.
DR PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..225
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 246..333
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 342 AA; 35418 MW; D44590C9845B8DBE CRC64;
MTALRIGART SPLARTQADW VAARLEALGV DCQFVGVTTA GDVDQRELTQ IGGTGVFVGA
VRSGLVRGTI DVAVHSLKDL PTADEDGLRV AAVPVREDVR DVVVGAGLAE LSERARSGRP
VRVGTGSPRR ASQLRQWAAD HDVALEVVPV RGNVDTRIGH VSGGELDATL LAAAGLRRLG
RLVHEQPDGA CRVVAGEGSV PAELVGTDVL LPAAGQGALA VEVAVDGGHD RLHLVDRLDD
PETRARVVAE RTFLATLEAG CLAPVGVLAS LSAPAAGASA TSQPQNLTLD AVIGRTIGSD
VDDRSGPELL RVRGAGPAQE ARRIGTELAE QALARLGDDL RR
//
