ID A0A1H8PU93_9FLAO Unreviewed; 305 AA.
AC A0A1H8PU93;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=SAMN04487942_2763 {ECO:0000313|EMBL:SEO45331.1};
OS Flavobacterium sinopsychrotolerans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=604089 {ECO:0000313|EMBL:SEO45331.1, ECO:0000313|Proteomes:UP000198657};
RN [1] {ECO:0000313|EMBL:SEO45331.1, ECO:0000313|Proteomes:UP000198657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8704 {ECO:0000313|EMBL:SEO45331.1,
RC ECO:0000313|Proteomes:UP000198657};
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; FODN01000007; SEO45331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PU93; -.
DR STRING; 604089.SAMN04487942_2763; -.
DR Proteomes; UP000198657; 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; cd13647; PBP2_PBGD_2; 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 5..204
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 220..288
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
SQ SEQUENCE 305 AA; 33834 MW; 6701F6419B521B41 CRC64;
MSKTIRIGTR DSELALWQAH TVEKKLNDLG YKTEILAVKS QGDIILDKPL YELGITGIFT
KTLDIAMING DVDIAVHSMK DVPTALPIGI VQAAVLERAN TLDILVHKGN LDFLNGEGTI
ATGSLRRQAQ WLNKYPNHKV VDLRGNVNTR MKKLQESDWN GAVFAAAGLE RINLKPSNYI
DLDWMIPAPA QGAMVVVAMA DDEFSRQALN ELNDIDTEVC THIERQFLKT LEGGCTAPIG
ALAVFVEDDI LFKGVLFSID GKQKIEIEKT VPMQEWKKLG FYCAKEILEN GGVELMTEIK
NNLKK
//
