(data stored in ACNUC7421 zone)

SWISSPROT: Q3IF72_PSEHT

ID   Q3IF72_PSEHT            Unreviewed;       312 AA.
AC   Q3IF72;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 100.
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:CAI85207.1};
GN   OrderedLocusNames=PSHAa0098 {ECO:0000313|EMBL:CAI85207.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85207.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85207.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC       hydroxymethylbilane pre-uroporphyrinogen in several discrete
CC       steps. {ECO:0000256|HAMAP-Rule:MF_00260,
CC       ECO:0000256|SAAS:SAAS00347445}.
CC   -!- CATALYTIC ACTIVITY: 4 porphobilinogen + H(2)O =
CC       hydroxymethylbilane + 4 NH(3). {ECO:0000256|HAMAP-Rule:MF_00260,
CC       ECO:0000256|SAAS:SAAS00347467}.
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-
CC       IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate:
CC       step 2/4. {ECO:0000256|HAMAP-Rule:MF_00260,
CC       ECO:0000256|SAAS:SAAS00635075}.
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|HAMAP-
CC       Rule:MF_00260, ECO:0000256|SAAS:SAAS00542451}.
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DR   EMBL; CR954246; CAI85207.1; -; Genomic_DNA.
DR   RefSeq; WP_011326825.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF72; -.
DR   STRING; 326442.PSHAa0098; -.
DR   EnsemblBacteria; CAI85207; CAI85207; PSHAa0098.
DR   KEGG; pha:PSHAa0098; -.
DR   PATRIC; fig|326442.8.peg.97; -.
DR   eggNOG; ENOG4105D6W; Bacteria.
DR   eggNOG; COG0181; LUCA.
DR   HOGENOM; HOG000228587; -.
DR   KO; K01749; -.
DR   OMA; CQVPIGV; -.
DR   OrthoDB; POG091H064B; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-HAMAP.
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   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;
DR   PRODOM; Q3IF72.
DR   SWISS-2DPAGE; Q3IF72.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00260,
KW   ECO:0000256|SAAS:SAAS00018392};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00260,
KW   ECO:0000256|SAAS:SAAS00018489, ECO:0000313|EMBL:CAI85207.1}.
FT   DOMAIN        8    215       Porphobil_deam. {ECO:0000259|Pfam:
FT                                PF01379}.
FT   DOMAIN      228    297       Porphobil_deamC. {ECO:0000259|Pfam:
FT                                PF03900}.
FT   MOD_RES     244    244       S-(dipyrrolylmethanemethyl)cysteine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00260}.
SQ   SEQUENCE   312 AA;  34104 MW;  937F73F00061310C CRC64;
     MTQTTNIVRI ATRKSALALW QAEFVKAQLE HYHPGILVEL VPMSTQGDII LDTPLAKIGG
     KGLFVKELEQ AMLEGLADMA VHSMKDMPVE FPEGLTLHTI CEREDPRDAF VSNNFANIDE
     LPQGAIVGTS SLRRQCQIRA SRPDLKIHDL RGNVNTRLAK LDSGQYDAII LAAAGLIRLE
     MKDRIRAYIE PEVSLPANGQ GAVGIECRTD DEAIKALLAP LEHSETRIRV NAERAMNRHL
     EGGCQVPIGA YALVNGDQVH LRGLVGAIDG SEILRDEVSG HVNDAEKLGV ELAKMLLAQG
     ADRILAEVYR DA
//

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