HEM3_SCHPO
ID HEM3_SCHPO Reviewed; 336 AA.
AC Q09899; P78887; Q9UT58;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
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=hem3; ORFNames=SPAC24B11.13, SPAC806.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; Evidence={ECO:0000250};
CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethan group.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR EMBL; D89238; BAA13899.1; -; mRNA.
DR EMBL; CU329670; CAB55280.1; -; Genomic_DNA.
DR PIR; T39093; T39093.
DR RefSeq; NP_001018179.1; NM_001018252.2.
DR AlphaFoldDB; Q09899; -.
DR SMR; Q09899; -.
DR BioGRID; 280459; 3.
DR STRING; 4896.SPAC24B11.13.1; -.
DR iPTMnet; Q09899; -.
DR MaxQB; Q09899; -.
DR PaxDb; Q09899; -.
DR PRIDE; Q09899; -.
DR EnsemblFungi; SPAC24B11.13.1; SPAC24B11.13.1:pep; SPAC24B11.13.
DR GeneID; 3361383; -.
DR KEGG; spo:SPAC24B11.13; -.
DR PomBase; SPAC24B11.13; hem3.
DR VEuPathDB; FungiDB:SPAC24B11.13; -.
DR eggNOG; KOG2892; Eukaryota.
DR HOGENOM; CLU_019704_0_2_1; -.
DR InParanoid; Q09899; -.
DR OMA; LWQANHI; -.
DR PhylomeDB; Q09899; -.
DR Reactome; R-SPO-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00319.
DR PRO; PR:Q09899; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; ISS:PomBase.
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 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 1: Evidence at protein level;
KW Heme biosynthesis; Phosphoprotein; Porphyrin biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..336
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000143043"
FT MOD_RES 251
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 20..24
FT /note="QSEII -> HQNY (in Ref. 1; BAA13899)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="Y -> N (in Ref. 1; BAA13899)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..55
FT /note="LF -> WL (in Ref. 1; BAA13899)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..98
FT /note="MPDGMV -> NARWYG (in Ref. 1; BAA13899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36827 MW; 512926BEEA3132B6 CRC64;
MPSCTSFPIG TRKSKLAVIQ SEIIREELEK HYPHLEFPII SRDTIGDEIL SKALFEFKRQ
LAKSLWTREL EALLVTNQCR ILVHSLKDLP SEMPDGMVIA CIPKRSCPLD AIVFKAGSHY
KTVADLPPGS VVGTSSIRRR ALLARNFPHL RFVDIRGNVG TRLAKLDAPD SQFDCLVLAA
AGLFRLGLKD RIAQMLTAPF VYYAVGQGAL AVEVRADDKE MIEMLKPLQH QETLYACLAE
RALMKRLQGG CAIPIGVQTD VLAISNSSYR ISLLGTVLSA DGLRAAFGNA EAVVSSEEEA
EELGITVALA LLKNGAGPIL EEHQRSSDSE ESLKNY
