ID A0A0L0JL42_9ACTN Unreviewed; 309 AA.
AC A0A0L0JL42;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=IQ63_37240 {ECO:0000313|EMBL:KND26343.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND26343.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KND26343.1}.
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DR EMBL; JPPY01000212; KND26343.1; -; Genomic_DNA.
DR RefSeq; WP_050374558.1; NZ_KQ257834.1.
DR AlphaFoldDB; A0A0L0JL42; -.
DR PATRIC; fig|42234.21.peg.7669; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000037151; Unassembled WGS sequence.
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 CDD; cd00494; PBP2_HMBS; 1.
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:UP000037151};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..210
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 225..294
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 309 AA; 32028 MW; 7DBB89BF68B46659 CRC64;
MTTYLVGSRA SKLAKAQVRQ YLELLRPRFP GITFTHRVIL EGGDRDRRSQ VSDVSAISGG
SAFSSEQEAA LSRGDVDVVI HSLKDLPTAN PSGLILLPPP GREDVRDALC GSTLAGLRKG
ARVGTGAARR VAQLLAVRPD LDVVPIRGNV PPRLKKIETM GLDAVVLAAA GLRRLGLDDA
IGELLPLDLF PPSPGQGALG VQVREDSVEL AEILSSVGDL AVDAQVRAER ALLAELHGGC
SVPVGAYAET APDGVLTLHA QVTSLDGSRR VSGTLSGSAG DAEKVGAGLA AELIGRGARA
ILDGIDVSR
//
