HEM3_PSEAE
ID HEM3_PSEAE Reviewed; 313 AA.
AC Q60169;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Porphobilinogen deaminase;
DE Short=PBG;
DE EC=2.5.1.61;
DE AltName: Full=Hydroxymethylbilane synthase;
DE Short=HMBS;
DE AltName: Full=Pre-uroporphyrinogen synthase;
GN Name=hemC; OrderedLocusNames=PA5260;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8159168; DOI=10.1007/bf00391011;
RA Mohr C.D., Sonsteby S.K., Deretic V.;
RT "The Pseudomonas aeruginosa homologs of hemC and hemD are linked to the
RT gene encoding the regulator of mucoidy AlgR.";
RL Mol. Gen. Genet. 242:177-184(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Note=Binds 1 dipyrromethane group covalently.;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR EMBL; M74844; AAA18907.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08645.1; -; Genomic_DNA.
DR PIR; B82989; B82989.
DR PIR; S41586; S41586.
DR RefSeq; NP_253947.1; NC_002516.2.
DR RefSeq; WP_003114031.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q60169; -.
DR SMR; Q60169; -.
DR STRING; 287.DR97_2631; -.
DR PaxDb; Q60169; -.
DR PRIDE; Q60169; -.
DR DNASU; 877673; -.
DR EnsemblBacteria; AAG08645; AAG08645; PA5260.
DR GeneID; 877673; -.
DR KEGG; pae:PA5260; -.
DR PATRIC; fig|208964.12.peg.5513; -.
DR PseudoCAP; PA5260; -.
DR HOGENOM; CLU_019704_0_2_6; -.
DR InParanoid; Q60169; -.
DR OMA; LWQANHI; -.
DR PhylomeDB; Q60169; -.
DR BioCyc; PAER208964:G1FZ6-5381-MON; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.160.40; -; 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 PANTHER; PTHR11557; PTHR11557; 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; SSF54782; SSF54782; 1.
DR TIGRFAMs; TIGR00212; hemC; 1.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000142974"
FT MOD_RES 242
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 24..26
FT /note="KAR -> NSTG (in Ref. 1; AAA18907)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..131
FT /note="SLR -> RLG (in Ref. 1; AAA18907)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> V (in Ref. 1; AAA18907)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="E -> D (in Ref. 1; AAA18907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 33641 MW; 2E35C71EA31BE07F CRC64;
MSSREIRIAT RQSALALWQA EYVKARLEQA HPGLTVTLLP MTSRGDKLLD APLAKIGGKG
LFVKELETAL LEGAADIAVH SMKDVPMDFP EGLGLYTICE REDPRDAFVS NTYASLEQLP
AGSVVGTSSL RRQAQLLARR PDLQIRFLRG NVNTRLAKLD AGEYDAIILA AAGLIRLGFE
SRIRSSISVD DSLPAGGQGA VGIECRTADS DLHALLEPLH HTDTALRVTA ERALNKRLNG
GCQVPIACYA IREGDQLWLR GLVGQPDGTQ LLRAEGRAPL AEAEALGVRV AEDLLEQGAE
AILEAVYGEA GHP
