ID A0A373NCW9_9FIRM Unreviewed; 810 AA.
AC A0A373NCW9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Porphobilinogen deaminase {ECO:0000256|HAMAP-Rule:MF_00260};
DE Short=PBG {ECO:0000256|HAMAP-Rule:MF_00260};
DE EC=2.5.1.61 {ECO:0000256|HAMAP-Rule:MF_00260};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|HAMAP-Rule:MF_00260};
DE Short=HMBS {ECO:0000256|HAMAP-Rule:MF_00260};
DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|HAMAP-Rule:MF_00260};
GN Name=hemC {ECO:0000256|HAMAP-Rule:MF_00260};
GN ORFNames=DWZ38_15160 {ECO:0000313|EMBL:RGF72395.1};
OS Ruminococcus sp. AF31-8BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=2293174 {ECO:0000313|EMBL:RGF72395.1, ECO:0000313|Proteomes:UP000262205};
RN [1] {ECO:0000313|EMBL:RGF72395.1, ECO:0000313|Proteomes:UP000262205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF31-8BH {ECO:0000313|EMBL:RGF72395.1,
RC ECO:0000313|Proteomes:UP000262205};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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, ECO:0000256|HAMAP-Rule:MF_00260}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00260};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00260};
CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000256|HAMAP-
CC Rule:MF_00260};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000256|HAMAP-
CC Rule:MF_00260}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|RuleBase:RU003960}.
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:RGF72395.1}.
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DR EMBL; QTVN01000012; RGF72395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A373NCW9; -.
DR OrthoDB; 9815856at2; -.
DR Proteomes; UP000262205; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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; cd00494; PBP2_HMBS; 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 HAMAP; MF_00260; Porphobil_deam; 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; 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 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; PF03900; Porphobil_deamC; 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; PS00533; PORPHOBILINOGEN_DEAM; 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, ECO:0000256|HAMAP-
KW Rule:MF_00260}; Reference proteome {ECO:0000313|Proteomes:UP000262205};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00260}.
FT DOMAIN 5..204
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 223..290
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT DOMAIN 310..521
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 572..797
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT MOD_RES 237
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ SEQUENCE 810 AA; 89241 MW; D771475879B213FD CRC64;
MSNKIVIGSR ESKLAVLQSQ MVQDFIVQNH PDMEVDILTM KTTGDKILDR TLDKIGGKGL
FVKELDRALL EGRSQLSVHS LKDMPMEESE ELPILAFSKR EDVRDVLVFP KGCEELDASK
PIGCSSLRRK LQLQEIFPDV KVKSIRGNLQ TRLEKLDSGE YSALVLAAAG LKRLGLEKRI
SRYFDTEEIL PAAGQGILAV QGKKGLDYEY LKGYDDPEAH SVALAERAFV RYLNGGCTSP
VAAYGQIQEG QLKLCGLYYE EETGHYLKGS KTGAVSEAEA LGIALAKELK ERCRKEYKVA
KQEERKEMGK VWLVGAGPGD AGLFTLKGAD VLEKADVVVY DSLVGQGILT RIPPDARLIN
VGKRAGHHMM PQNMINQVLA DEAKKGNRVV RLKGGDPFLF GRGGEELELL TKEGVPYEVV
PGVTSPISVP AYNGIPVTHR DFCSSVHIIT GHKRQGMEYD IDFKALVHTK GTLVFLMGLT
AMEDICKGLM EAGMDPDMPA AVLSKGTTAG QRRVIATIST LKKESDRQKI KTPAIIVVGK
VCTLSEDFAW YEKLPLAGWK ILVTRPRENI SRTAAKLREK GAEVLELPSI SISPLEDQSR
LQEAFAKLNT YDWLVFTSPA GVEVFWRELG KKKVDIRCLG SVKIAAIGEG TKKKLLERGI
YADFVPSVYD GDTLGKELAS LLTGKEKILI PRAMLGNKTL VEELEKTGAS VEDVPTYETD
YQNCPLIDEK KEFEEGSIDM VVFTSASTVK GFVKSTNGLD YSRVRAACIG KQTKAAADAY
GMQTYMSEKA TIDSLIELVE TLKRSEEKWN
//
