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Entry: I0AGZ7_IGNAJ
LinkDB: I0AGZ7_IGNAJ
Original site: I0AGZ7_IGNAJ 
ID   I0AGZ7_IGNAJ            Unreviewed;       312 AA.
AC   I0AGZ7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   ECO:0000313|EMBL:AFH48254.1};
GN   OrderedLocusNames=IALB_0542 {ECO:0000313|EMBL:AFH48254.1};
OS   Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS   Mat9-16).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Ignavibacteriaceae; Ignavibacterium.
OX   NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48254.1, ECO:0000313|Proteomes:UP000007394};
RN   [1] {ECO:0000313|EMBL:AFH48254.1, ECO:0000313|Proteomes:UP000007394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC   {ECO:0000313|Proteomes:UP000007394};
RX   PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA   Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA   Bryant D.A.;
RT   "Complete genome of Ignavibacterium album, a metabolically versatile,
RT   flagellated, facultative anaerobe from the phylum Chlorobi.";
RL   Front. Microbiol. 3:185-185(2012).
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000256|HAMAP-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|ARBA:ARBA00005638,
CC       ECO:0000256|HAMAP-Rule:MF_00260}.
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DR   EMBL; CP003418; AFH48254.1; -; Genomic_DNA.
DR   RefSeq; WP_014559412.1; NC_017464.1.
DR   AlphaFoldDB; I0AGZ7; -.
DR   STRING; 945713.IALB_0542; -.
DR   GeneID; 78242279; -.
DR   KEGG; ial:IALB_0542; -.
DR   PATRIC; fig|945713.3.peg.542; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_0_2_10; -.
DR   OrthoDB; 9810298at2; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000007394; Chromosome.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13646; PBP2_EcHMBS_like; 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   HAMAP; MF_00260; Porphobil_deam; 1.
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; PF01379; Porphobil_deam; 1.
DR   Pfam; PF03900; Porphobil_deamC; 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.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00260}; Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          6..211
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          226..295
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   MOD_RES         242
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   312 AA;  34611 MW;  C93AEC5D665C3656 CRC64;
     MNKKLLIGSR GSELALWQAN FVKKELEKKH RGLSVEIKII KTKGDKILDV ALSKIGDKSL
     FTKELEVELL SKRIDIAVHS LKDLQTQIPE GLKLAAVTKR HDVEDVLIAR KKGLTIHTLP
     ENAVVATGSL RRRAQLQHLR PDIKVVDLRG NVPSRIKKFL ESDWDAIILA RAGVERLGLK
     KYISSYISKE EILPAVGQGA LGIEIHTDNQ FAEEILQSIH HQNTFTAVSA ERALLRALEG
     GCQVPIGAFA EVQSNGLYLD AMVGSLDGSI TFRKKVRGRK DEPEKLGRSL AKDLLKAGAK
     DILDEVYNNS RK
//
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