ID A0A1M3MFI5_9BACT Unreviewed; 702 AA.
AC A0A1M3MFI5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=uroporphyrinogen-III C-methyltransferase {ECO:0000256|ARBA:ARBA00012162};
DE EC=2.1.1.107 {ECO:0000256|ARBA:ARBA00012162};
GN ORFNames=BGP01_07410 {ECO:0000313|EMBL:OJX92435.1};
OS Paludibacter sp. 47-17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX92435.1, ECO:0000313|Proteomes:UP000183960};
RN [1] {ECO:0000313|EMBL:OJX92435.1, ECO:0000313|Proteomes:UP000183960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-17 {ECO:0000313|EMBL:OJX92435.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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 -!- 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:OJX92435.1}.
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DR EMBL; MKVT01000001; OJX92435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3MFI5; -.
DR STRING; 1895899.BGP01_07410; -.
DR Proteomes; UP000183960; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR CDD; cd06578; HemD; 1.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 3.40.50.10090; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR006366; CobA/CysG_C.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
DR NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR Pfam; PF02602; HEM4; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF69618; HemD-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OJX92435.1};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OJX92435.1}.
FT DOMAIN 6..202
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 230..430
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 476..658
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
SQ SEQUENCE 702 AA; 76775 MW; A2AE4AA137704A80 CRC64;
MASELIRVAS RTSTLALLQV REFFNAFPGV AYEIIGRPAW GDLRKDISLL DNPPADLFTR
EQDELVLLGE ADIAIHSAKD MPFPLPDGLE LIALTEAFDT SDSLVSRDNK TLAELPAGAR
IATSSPTRKA GLLAIRPELV VAGIRGTIEE RIAQIDAGDY DALIVATCAL KRLGLMHRVA
EVLPFRTHPL QGSLAVVGRK GNPLFSRKEM RDRAEVNFAT ADARSRYGHV SITGFGPGNP
DLLTRRATRA LGLADIIFYD DLLDARELHR YTAEKVYVGK RKDRHSHSQE DIHQLMIDAA
RAGRRVVRLK GGDPMVFAHG GEEALALAQC YIPYEIIPGI STALAVASLT GIPLTHRGLA
ASVAFVTGHS PQLQLPGTDT VVIYMGAANL RPIATNALAQ GRTPETPVLL AAHVSRNNEQ
RFFTTLGQLA SEDNNYPTPL IAVVGKVAGL GAVLPAKSRP TLLVTGTHPG DYDRLGKVIH
QPLIELKALD TPPLGELLRH HDWLIFTSRN SVDFFVRALL KEEKTDLRSL AGLRIVSVGR
ITSRTLLRYG LKPDLQATDE SSEGILTLLR HRPAARAVIP RSAIGLPALP EGLRKAGWKI
TEISLYTNNL PEPTEAIDLT GIDTIVLTSP SCVTNFKKVY GQFPAEKNYL LRGRETEKRF
ENEKDNTKNY QVKLQLSGHT NTDAAAMAES TRHPLHHQHD SI
//
