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Database: UniProt
Entry: A0A1K1M6V1_9FIRM
LinkDB: A0A1K1M6V1_9FIRM
Original site: A0A1K1M6V1_9FIRM 
ID   A0A1K1M6V1_9FIRM        Unreviewed;       290 AA.
AC   A0A1K1M6V1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE            EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN   ORFNames=SAMN02910447_00652 {ECO:0000313|EMBL:SFW18906.1};
OS   Ruminococcus sp. YE71.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW18906.1, ECO:0000313|Proteomes:UP000182164};
RN   [1] {ECO:0000313|EMBL:SFW18906.1, ECO:0000313|Proteomes:UP000182164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE71 {ECO:0000313|EMBL:SFW18906.1,
RC   ECO:0000313|Proteomes:UP000182164};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the HMBS family.
CC       {ECO:0000256|ARBA:ARBA00005638}.
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DR   EMBL; FPIR01000003; SFW18906.1; -; Genomic_DNA.
DR   RefSeq; WP_072416787.1; NZ_FPIR01000003.1.
DR   AlphaFoldDB; A0A1K1M6V1; -.
DR   STRING; 244362.SAMN02910447_00652; -.
DR   Proteomes; UP000182164; Unassembled WGS sequence.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd13647; PBP2_PBGD_2; 1.
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; IPR000860; HemC.
DR   InterPro; IPR022417; Porphobilin_deaminase_N.
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; PF01379; Porphobil_deam; 1.
DR   PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182164};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..213
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
SQ   SEQUENCE   290 AA;  31576 MW;  7EC9D2F849BF775F CRC64;
     MINKIRIGTR GSRLALAQTE LVKTAVRSRF PDIECETVVI KTKGDIVKEK PIAELGGAGV
     FAAEIEKALA EGDIDLAVHS AKDLPTALLA GNEIRCVLRR ADPRDVIIYR KGIDYTFRNP
     KIGTSSVRRR SGFTRLFPAT VPRFLDIRGN IDTRIEKLRS GKYDAIILAA AGLERLGLLT
     IDDSELGCEI LPADRFLPAP CQAIIAAESR AGELTEILDR VNDAETFVSF NTERYVLELL
     GGDCSQPIGA YSYVKDGRLV LSVSNGGASV TAEGDVNEYR ELAEGLVKQL
//
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