ID A0A1B6YC25_9BACT Unreviewed; 297 AA.
AC A0A1B6YC25;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=A8B79_01745 {ECO:0000313|EMBL:OAN62974.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN62974.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN62974.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN62974.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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}.
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:OAN62974.1}.
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DR EMBL; LXYG01000012; OAN62974.1; -; Genomic_DNA.
DR RefSeq; WP_066218795.1; NZ_LXYG01000012.1.
DR AlphaFoldDB; A0A1B6YC25; -.
DR STRING; 1849360.A8B79_01745; -.
DR InParanoid; A0A1B6YC25; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000078514; 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 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:UP000078514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..199
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 216..286
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 297 AA; 32551 MW; 1D9B8C352DCC6D01 CRC64;
MKLKIGTRRS KLALWQSNLV AKKLNALDVQ TELVEIESFG DKEQDLPLHK LGDKGVFTKA
LDDALLDGKI DLAVHSLKDV PTIFEDGLQL NAVLERANPI DVLVEPLNYE KGNASRTIAT
GSIRRSAFWK NKYPEDEVVD LRGNVPTRLN KVDTLGWDGA IFAHAGLERL GLGERISKEL
PWMISAPSQG AIGIVSKEDF KYSEIVSVLN DDNTRICVDI ERAFLRTLDA GCSSPVGALA
EVKGDTLFFK GAVLSVDGKQ RVDIQEEIEL RNANETLGAE FAKKVINEGA ADLLNGN
//
