ID A0A368P8Y3_9FLAO Unreviewed; 529 AA.
AC A0A368P8Y3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=DU428_02455 {ECO:0000313|EMBL:RCU58259.1};
OS Oceanihabitans sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Oceanihabitans.
OX NCBI_TaxID=1812012 {ECO:0000313|EMBL:RCU58259.1, ECO:0000313|Proteomes:UP000252249};
RN [1] {ECO:0000313|EMBL:RCU58259.1, ECO:0000313|Proteomes:UP000252249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9-10 {ECO:0000313|EMBL:RCU58259.1,
RC ECO:0000313|Proteomes:UP000252249};
RA Li C.-M.;
RT "Oceanihabitans testaceum sp. nov., isolated from marine sediment.";
RL Submitted (JUL-2018) 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:RCU58259.1}.
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DR EMBL; QPIG01000001; RCU58259.1; -; Genomic_DNA.
DR RefSeq; WP_072347988.1; NZ_QPIG01000001.1.
DR AlphaFoldDB; A0A368P8Y3; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000252249; Unassembled WGS sequence.
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:UP000252249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RCU58259.1}.
FT DOMAIN 5..208
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 222..275
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT DOMAIN 351..519
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
SQ SEQUENCE 529 AA; 59568 MW; E7C12083F7FFDEDF CRC64;
MSKIIRIGTR DSELALYQAN VVKKQLEDLG HKTEIVPVKS TGDLVLNKPL YKLGITGVFT
KTLDIAMLNY DIDIAVHSSK DVPTDLPEGI VQAAVIKRGN VRDTLVFKQN EEFLSSKHAV
IATGSLRRKA QWLNRFPTHT IEDIRGNVNL RLQKLEDNEH WNATIFAAAG LGRIGKRPEN
AINLDWMIPA PAQGAIMITA LEEDEEILAI CKEINHEETE ICTSIEREFL NRLEGGCTAP
IGALAFIKDE EVTFEAVLLS QDGQKKIEVK RVEKLGEHHN IAKYSADYII ERGGKRLMDS
LTRAEKLSKV YSTKSLTERQ RLLVNQNLLV ESSDFIKINI NRLKPQVVRK PIKNVIITSQ
NTVEALLQNY SPAELQFENI YCVGRRTKRL VEKRIGKVNH AEPNAKKLAA YLIEYLEGTE
VTYFCSNLHL DTLPTVLAEN NIEVNEVIAY ETKLDPIKLK DTVEGVMFYS PSTVQSFKQE
NIAKEGMIAF CIGETTAHEA SKHFADVRIS KIPTVESVIE LVNEHYAKQ
//
