ID A0A1M4S3L4_9ACTO Unreviewed; 395 AA.
AC A0A1M4S3L4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=ACGLYG10_3050 {ECO:0000313|EMBL:SHE26795.1};
OS Actinomyces glycerinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1892869 {ECO:0000313|EMBL:SHE26795.1, ECO:0000313|Proteomes:UP000184291};
RN [1] {ECO:0000313|Proteomes:UP000184291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Strepis N.;
RL Submitted (SEP-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; FQTT01000016; SHE26795.1; -; Genomic_DNA.
DR RefSeq; WP_073333858.1; NZ_FQTT01000016.1.
DR AlphaFoldDB; A0A1M4S3L4; -.
DR STRING; 1892869.ACGLYG10_3050; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000184291; 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 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 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:UP000184291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..253
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 299..372
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 395 AA; 39087 MW; B86C6CFC07AEC83A CRC64;
MNAGTTIGAG GPAARTVRLG TRGSALAVAQ STQVARALAA ASRRIGADLE VELVQIRTRG
DVDATPLTRL GGVGVFAAAL REALLAGACD LAVHSCKDLP TAAVPGLRIA AVPAREDPRD
ALCTADGRTL ADLPRGARVG TGSPRRGAQL LAVRPDLEVV PVRGNVPTRL SRVVGAVVGA
DGPLGAVREP DLDAVVLALA GLRRLGLDGY ATQPLALPQT EIAGTGVVDP ADPAPIMVPA
PAQGALALET RDEAGAGADP SGVAAGVEPL VGGAGRDPGL AAALAAALAE LDDPVTHAAV
AAERALMRRL EAGCAAPVGA VAVPAPRADG SSGLRLDAVV AAADGTRLLR ESAVGDQAEP
AGLGEAVAEA LLSAGAAQLV DLHASLPDRG RREAP
//
