ID A0A1G8DPM8_9MICO Unreviewed; 308 AA.
AC A0A1G8DPM8;
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=SAMN04489720_1721 {ECO:0000313|EMBL:SDH59449.1};
OS Agrococcus jejuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=399736 {ECO:0000313|EMBL:SDH59449.1, ECO:0000313|Proteomes:UP000198822};
RN [1] {ECO:0000313|EMBL:SDH59449.1, ECO:0000313|Proteomes:UP000198822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22002 {ECO:0000313|EMBL:SDH59449.1,
RC ECO:0000313|Proteomes:UP000198822};
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; LT629695; SDH59449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8DPM8; -.
DR STRING; 399736.SAMN04489720_1721; -.
DR Proteomes; UP000198822; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..205
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 221..264
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 308 AA; 31599 MW; FECB70E6E5725AFD CRC64;
MSALRVGTRG SALALAQTTA LAARFAGEVE IVEITTQGDV DRAPLAQIGG TGVFTSALRE
ALLADEVDVI VHSMKDLPTA PHPGIVLAAV AKREDARDAL CARDGLGFDD LPEGAKVGTG
SPRRAAQLRR VRPDLDVVDI RGNVETRLAR AQGPDADLDA VVLALAGLTR LGRTDAVTEV
LSLGRFPTAP AQGALAVETR DGDAASIRAV AKADHAVTRA CADAERLVLA GLEAGCSAPI
AASAQVDDGM LFLTATVYAL DGSKHLTASH AYTLDGQSGP ELSEAAMDVA GRAVRELVDA
GAMELDAA
//