ID A0A1Y0MJA2_9FLAO Unreviewed; 525 AA.
AC A0A1Y0MJA2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=BTO05_08140 {ECO:0000313|EMBL:ARV09609.1};
OS Winogradskyella sp. PC-19.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754417 {ECO:0000313|EMBL:ARV09609.1, ECO:0000313|Proteomes:UP000195547};
RN [1] {ECO:0000313|EMBL:ARV09609.1, ECO:0000313|Proteomes:UP000195547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC-19 {ECO:0000313|EMBL:ARV09609.1,
RC ECO:0000313|Proteomes:UP000195547};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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; CP019332; ARV09609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MJA2; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000195547; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06578; HemD; 1.
DR CDD; cd13647; PBP2_PBGD_2; 1.
DR Gene3D; 3.40.50.10090; -; 2.
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; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
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; PF02602; HEM4; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF69618; HemD-like; 1.
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:UP000195547};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..207
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 224..272
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT DOMAIN 335..517
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
SQ SEQUENCE 525 AA; 58583 MW; 0F0E1B28339A998D CRC64;
MSRIIRIGTR DSQLAMWQAK TVQSQLEHLG HKTVLVPVKS TGDIVLDKPL YELGITGIFT
KTLDIAMLNG DIDIAVHSLK DVPTILPKGI VQAAVLKRGN INDTLVFKKN EEFLSAKDAV
IATGSLRRRA QWLNRYPTHT IVGLRGNVNS RLEKLENNDW NGAIFAGAGL GRLNITPENS
INLHWMIPAP AQGAVMVAAL EEDDEVREIC AEINHRETEI GTSIEREFLN RLEGGCTAPI
GAICYVNKDD EVHFKGILLS KDGSRKIEVT KVVPLGKHDG IAEFCANYII EKGGKTLIDQ
LQRSDKTTNI YSTKTLTEDQ KLLFHNDVVS DSNDAIKISL NRIHKKVVRN EIQNVIITSQ
NAVEALLTSF SAVELQFKNI YCVGRRTKRM VEKRIGKVTH MAPNAKRLAE YLVEYIDGTE
VTYFCSDLRL DDLPNILTEN NITVNEVEAY QTKYDAVKLE NNVDGIMFYS PSTIDSFLKQ
NKANGIAFCI GETTANTAKK HFEDVRVAKV PTVESVIELV NEYYA
//
