ID D4JBU7_9FIRM Unreviewed; 799 AA.
AC D4JBU7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=uroporphyrinogen-III C-methyltransferase {ECO:0000256|ARBA:ARBA00012162};
DE EC=2.1.1.107 {ECO:0000256|ARBA:ARBA00012162};
GN ORFNames=CC1_32790 {ECO:0000313|EMBL:CBK81818.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81818.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK81818.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81818.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK81818.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81818.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-2010) 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 -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|RuleBase:RU003960}.
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DR EMBL; FP929038; CBK81818.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JBU7; -.
DR STRING; 717962.CC1_32790; -.
DR KEGG; cct:CC1_32790; -.
DR PATRIC; fig|717962.3.peg.3150; -.
DR HOGENOM; CLU_351875_0_0_9; -.
DR Proteomes; UP000008798; Chromosome.
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; -; 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; 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 InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR NCBIfam; TIGR00212; hemC; 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; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU003960};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 1..211
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 304..516
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 567..787
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
SQ SEQUENCE 799 AA; 87356 MW; 1327B2F6D5CAF99F CRC64;
MVQTEMAAEA IKKVFPSIEI EIAGFETKGD RHLDKSLSAF GSKGAFTKEL EGAMLDGRID
LAVHSAKDLP VELPEGLTVG AVLKRGDSRD VWVSLRREFS IIEECKEKTV VGTGSLRRAL
QIQQICPGVD IRDIRGNVPT RLKKLSDGMY DGIILAAAGL KRLGYLSEDC ETEGSFEAEE
QTFFYEILSK EQFLPAAGQG IIALETRQKD CEDCMQAIHD EDTWQMFLTE RSFLRAIGGG
CNEAAAVDVR MDGQKVSVRA RYAGDGLHMK EKTVTGTRCG NIEEDRKLAV SLGEQMAARL
QNGKVYLIGA GPGDTGLITM KGMEALKEAD VIVYDHLASP SLLNATKDEA EWIDAGKFAG
HHRMKQAEIE ELLIEKAMEG QTVARLKGGD PFIFGRGGEE ALALTAAGIE YEVIPGVSSA
YSAPAYAGIP ITHRGKASSF HVITGHEDPT KENSSLDYEI LAREEGTLVF LMGLSRLHQI
SERLIANGKD AHTPAAVIAS GTTARQRCVT GKLGRIAAIS EKADIQPPAI LVVGDVVSLK
KEIDWQQAGA LSGKKILVTA TEIIAEPLAE KIRKLGGEPV VMSLISVRAE KMYGLKEVLV
RPGKRWLVFT SRNGVRFFFE QMKKEEIDIR ILGICRIAVM GAGTRRELEN WGCYADLMPE
QSCSESLAKA LCENVQYDEE ICLFRAEEAS DVLIKRLREK GFFVVDTPMY HTEKMWKKAA
LLKEVLEDMD AVTFCSASAV RAFAQMTEGQ RFAAKNVCIG PVTAEAAEKA DISIDKIAGQ
YDLEGLAAAL CDILCRNES
//
