HEM31_STRAW
ID HEM31_STRAW Reviewed; 324 AA.
AC Q82E76;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Porphobilinogen deaminase 1;
DE Short=PBG 1;
DE EC=2.5.1.61;
DE AltName: Full=Hydroxymethylbilane synthase 1;
DE Short=HMBS 1;
DE AltName: Full=Pre-uroporphyrinogen synthase 1;
GN Name=hemC1; OrderedLocusNames=SAV_4740;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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 -!- 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; BA000030; BAC72452.1; -; Genomic_DNA.
DR RefSeq; WP_010986163.1; NZ_JZJK01000077.1.
DR AlphaFoldDB; Q82E76; -.
DR SMR; Q82E76; -.
DR STRING; 227882.SAV_4740; -.
DR EnsemblBacteria; BAC72452; BAC72452; SAVERM_4740.
DR KEGG; sma:SAVERM_4740; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_1_0_11; -.
DR OMA; LWQANHI; -.
DR OrthoDB; 1450400at2; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
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..324
FT /note="Porphobilinogen deaminase 1"
FT /id="PRO_0000142997"
FT MOD_RES 249
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 33772 MW; D705424396B0B775 CRC64;
MSEQALRLGT RRSKLAMAQS GQVADAVRQV TGRPVELVEI TTYGDTSREH LAQIGGTGVF
VTALRDALLR GEVDFAVHSL KDLPTAQPDE LALAAVPVRE DPRDVLVARD GLTFEELGAP
SPKGTARVGT GSPRRMAQLN AYARSHGLAV ETVPIRGNVD SRIGYVRSGE LDGVVLAAAG
LHRIGRIDEV TEFLPVDTVL PAPGQGALAI ECAADNADLI AALAELDDPF TRAAVTAERS
LLAALEAGCS APVGALADLL ADGQIVTEMR LRGVVGTTDG STLVQLSTTG PVPETHDQAM
ALGRELAAEM LAKGAAGLMG EREH