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Database: UniProt
Entry: A0A0Q4XU37_9BURK
LinkDB: A0A0Q4XU37_9BURK
Original site: A0A0Q4XU37_9BURK 
ID   A0A0Q4XU37_9BURK        Unreviewed;       305 AA.
AC   A0A0Q4XU37;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ASF43_15855 {ECO:0000313|EMBL:KQP14290.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP14290.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP14290.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14290.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP14290.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14290.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004735}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       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}.
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:KQP14290.1}.
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DR   EMBL; LMMV01000022; KQP14290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4XU37; -.
DR   STRING; 1736316.ASF43_15855; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000051560; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00260}; Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          9..213
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          226..300
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   MOD_RES         243
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   305 AA;  32440 MW;  25209DFA195886BA CRC64;
     MPAPSPKPIV IATRESRLAL WQAEHVQSLL EQRGLQVSLL GMTTRGDQIL DRTLSKVGGK
     GLFVKELENA LEDGRADIAV HSLKDVPMEL PDGFVLACVL EREDPRDAFV SPHFARLADL
     PQGAVVGTSS LRRSVLLKAL RPDLDIQPLR GNLDTRLRKL DEGHYAAIVL AAAGLKRLGL
     HARVREVFEP DAMLPAAGQG ALGIEVRAGR QDLLELLAPL AHSGSWLAVT AERAVSRAMG
     GSCSMPLAAH ARWLGDTLRL QAAWGDAETW APLVQVETAG QVADACGAEA LGTQVAAQLR
     AGGAA
//
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