ID A0A1V3L7N7_9PAST Unreviewed; 313 AA.
AC A0A1V3L7N7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BKG88_06005 {ECO:0000313|EMBL:OOF85952.1}, BKG92_10465
GN {ECO:0000313|EMBL:OOF80483.1};
OS Rodentibacter ratti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1906745 {ECO:0000313|EMBL:OOF85952.1, ECO:0000313|Proteomes:UP000189353};
RN [1] {ECO:0000313|Proteomes:UP000188573, ECO:0000313|Proteomes:UP000189353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac81 {ECO:0000313|EMBL:OOF80483.1,
RC ECO:0000313|Proteomes:UP000188573}, and Ppn158
RC {ECO:0000313|EMBL:OOF85952.1, ECO:0000313|Proteomes:UP000189353};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
RL Submitted (OCT-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, 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:OOF85952.1}.
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DR EMBL; MLAG01000064; OOF80483.1; -; Genomic_DNA.
DR EMBL; MLAI01000016; OOF85952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3L7N7; -.
DR OrthoDB; 9810298at2; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000188573; Unassembled WGS sequence.
DR Proteomes; UP000189353; 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; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00260}.
FT DOMAIN 7..213
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 227..296
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 313 AA; 33899 MW; FFE55D5468178BA6 CRC64;
MTTPTILKIA TRQSPLALWQ ANFVKERLEN IHPALTVELV PMVTKGDIIL DTPLAKIGGK
GLFVKELENA LLEKRADIAV HSMKDVPMQF PEGLGLSVIC KREDPRDAFV SNHYASFEDL
PKGAIVGTSS LRRQCQLKQL RPDLDIRSLR GNVGTRLNKL DNGEYDAIIL AAAGLIRLGM
QARITSFIDV TTSLPASGQG AVGIECRTDD LLVQELLAPL ADEETTVCVK AERAMNARLQ
GGCQVPIGGY AVLENNQIRL TALVGELDGS SIIRAEGKNA VEKAEELGVQ IAEQLLAQGA
DRILAKVYEL GDK
//